iAF1261_ecocyc_comments_of_gene = {('B0433', 'AGM4Pt2pp') : """(AmpG is a member of the major facilitator superfamily of transporters,
and together with AmpD, is essential for induction of the AmpC Β-lactamase
and is involved in the recycling of cell wall peptides
|CITS: [90120556] [94049112] [95291453] [96100441]|.
Mutants in ampG are unable to induce ampC and display greatly
increased cell wall turnover |CITS: [95009971]|.
AmpG is responsible for the transport of precursors of the anhMurNAc tripeptide into the cytoplasm
|CITS:[8878601]|. These precursors are the products of peptidoglycan degradation and include the
disaccharide GlcNAc-anhMurNAc as well as GlcNAc-anhMurNAc-oligopeptides (tri-, tetra-, and
pentapeptides). Transport is dependent on the proton motive force |CITS:[12426329]|.
Following uptake of these muropeptides, they are degraded, releasing the components which can
subsequently be used in cell wall synthesis |CITS: [95302966]|.
Experiments with β-lactamase fusions show AmpG contains two large cytoplasmic loops and 10
transmembrane segments |CITS:[15728916]|.
Cytosolic muramyl peptides probably induce expression of ampC by binding
to its regulator AmpR |CITS: [97302495]|.)""",
('B2835', '2AGPG141tipp') : """(LplT is a major facilitator superfamily (MFS) protein that acts as a flippase for transbilayer movement of
lysophospholipids. Mutation experiments and
transporter assays have determined LplT is responsible for the facilitated diffusion of lysophospholipids to
the cytoplasmic portion of the inner membrane providing substrate for the bifunctional enzyme
2-acyl-GPE acyltransferase/acyl-ACP synthetase (Aas). lplT forms an operon with the aas
gene |CITS:[15661733]|.)""",
('B2979', 'GLYCTO4') : """(E. coli cells harboring a plasmid containing glcDEF have glycolate oxidase activity in crude cell extracts;
an insertion mutant in either glcD, glcE or glcF abolishes this activity |CITS: [8606183]|.)""",
('B4467', 'GLYCTO4') : """(E. coli cells harboring a plasmid containing glcDEF have glycolate oxidase activity in crude cell extracts;
an insertion mutant in either glcD, glcE or glcF abolishes this activity |CITS: [8606183]|.)""",
('B4468', 'GLYCTO4') : """(E. coli cells harboring a plasmid containing glcDEF have glycolate oxidase activity in crude cell extracts;
an insertion mutant in either glcD, glcE or glcF abolishes this activity |CITS: [8606183]|.)""",
('B2979', 'GLYCTO3') : """(E. coli cells harboring a plasmid containing glcDEF have glycolate oxidase activity in crude cell extracts;
an insertion mutant in either glcD, glcE or glcF abolishes this activity |CITS: [8606183]|.)""",
('B4467', 'GLYCTO3') : """(E. coli cells harboring a plasmid containing glcDEF have glycolate oxidase activity in crude cell extracts;
an insertion mutant in either glcD, glcE or glcF abolishes this activity |CITS: [8606183]|.)""",
('B4468', 'GLYCTO3') : """(E. coli cells harboring a plasmid containing glcDEF have glycolate oxidase activity in crude cell extracts;
an insertion mutant in either glcD, glcE or glcF abolishes this activity |CITS: [8606183]|.)""",
('B2979', 'GLYCTO2') : """(E. coli cells harboring a plasmid containing glcDEF have glycolate oxidase activity in crude cell extracts;
an insertion mutant in either glcD, glcE or glcF abolishes this activity |CITS: [8606183]|.)""",
('B4467', 'GLYCTO2') : """(E. coli cells harboring a plasmid containing glcDEF have glycolate oxidase activity in crude cell extracts;
an insertion mutant in either glcD, glcE or glcF abolishes this activity |CITS: [8606183]|.)""",
('B4468', 'GLYCTO2') : """(E. coli cells harboring a plasmid containing glcDEF have glycolate oxidase activity in crude cell extracts;
an insertion mutant in either glcD, glcE or glcF abolishes this activity |CITS: [8606183]|.)""",
('B3469', 'COBALT2abcpp') : """(The gene product of the yhhO gene, also referred to as zntA, is
a P-type ATPase involved in the efflux of Pb(II), Cd(II), and Zn(II) |CITS:[98070750] [20263730]|.
ZntA displays a Km of approximately 20 μM for Cd(II) and
100 μM for Zn(II) |CITS:[20127859]|. The transporter appears to be inhibited
by vanadate, a common inhibitor of P-type ATPase. The ATPase activity of the
transporter was found to follow the order Pb(II), Cd(II), Zn(II), and Hg(II) |CITS:[20127859]|.
A zntA mutant showed hypersensitivity to Cd(II) and Zn(II) |CITS:[98070750]|.
The zntA gene was found to be under the control of the transcriptional
regulator ZntR. zntA expression is activated by an increased concentration
of Cd(II) and Zn(II) within the cell, showing greater induction by Cd(II) than by
Zn(II) |CITS:[20127859]|.)""",
('B2789', 'GALCTt2rpp') : """(The YgcZ protein may function as a glucarate transporter. The
ygcZ gene is encoded in a probable operon with genes
encoding two subunits of a putative glucarate dehydratase. YgcZ
is a member of the major facilitator superfamily (MFS) of
transporters |CITS: [98190790]| and shares a high level of sequence
similarity with probable glucarate transporters from various
organisms. YgcZ probably functions as a glucarate/proton transporter.)""",
('B3127', 'GALCTt2rpp') : """(YhaU is an uncharacterised member of the major facilitator superfamily (MFS)
of transporters |CITS: [98190790]|.
Based on sequence similarity, YhaU may function as a proton-driven
glucarate uptake system.)""",
('B0839', 'MDDCP2pp') : """(DacC is a penicillin-binding protein that is required for proper cell morphology and provides
some resistance to penicillin |CITS: [1447130][12354237][6215397]|. It is one of four DD-carboxypeptidase
low-molecular weight PBPs in Escherichia coli (along with PBP4, PBP6 and DacD) that modify
peptidoglycans through the removal of the terminal D-alanine from pentapeptide side chains |CITS:[368033]|,
|CITS:[8955390]|.
The carboxy-terminus of DacC is capable of forming an alpha helix and interacts with
membranes chiefly through hydrophobic forces |CITS: [9371419][9858668]|.
Deletion of this membrane-anchoring portion of the protein produces soluble DacC. Whereas
overexpression of native DacC results in membrane vesicles in the cystoplasm, overexpression
of this soluble variant yields inclusion bodies. Both forms of DacC can be purified with
Procion rubine MX-B and subsequently bind stoichiometrically with penicillin |CITS: [1447130]|.
Despite being part of a family of D-alanine carboxypeptidases, DacC lacks detectable activity
against bisacetyl-L-lysine-D-alanyl-D-alanine and other test substrates |CITS: [1447130]|.
Deletions in dacC are viable, though slightly penicillin sensitive |CITS: [6215397]|.
dacC dacA double mutants are viable, though they show defects in morphology and cell division
when bolA, which is required for dacC expression on entry to stationary phase, is overexpressed |CITS: [3903044][12354237][2684651]|.
A complete deletion of dacA-D is also viable, as is a strain lacking eight of the known penicillin-binding protein genes,
dacC among them |CITS: [8955390][10383966]|. Overexpression of DacC allows cell division in ftsI23 mutants, but leads to cell
lysis during early exponential growth |CITS: [2254246][11325933]|.)""",
('B1800', 'MALDDH') : """(No information about this protein was found by a literature search conducted on December 28, 2005.
)""",
('B2835', '2AGPG120tipp') : """(LplT is a major facilitator superfamily (MFS) protein that acts as a flippase for transbilayer movement of
lysophospholipids. Mutation experiments and
transporter assays have determined LplT is responsible for the facilitated diffusion of lysophospholipids to
the cytoplasmic portion of the inner membrane providing substrate for the bifunctional enzyme
2-acyl-GPE acyltransferase/acyl-ACP synthetase (Aas). lplT forms an operon with the aas
gene |CITS:[15661733]|.)""",
('B1193', 'MLTGY3pp') : """(EmtA is a lytic endotransglycosylase which is expressed in Escherichia coli as a membrane-bound lipoprotein.
Overexpression of emtA results in the hydrolysis of glycan strands isolated from the murein (peptidoglycan)
sacculus, which serves as a bacterial exoskeleton |CITS:[9642199]|. It is believed that the emtA gene product,
like other murein hydrolases, is involved in cleavage of the net-like murein structure thereby allowing for cell enlargement
and division and also for localized opening of the peptidoglycan layer to allow the export of bulky compounds such as DNA,
toxins, flagella, and fimbrial proteins |CITS:[8824596]|, |CITS:[9642199]|.)""",
('B2963', 'MLTGY3pp') : """(E. coli contains a large number of murein hydrolase enzymes. MltC belongs to the family of lytic
transglycosylases which degrade GlcNAcMurNAc glycan strands, resulting in the formation of a
1,6-anhydro-MurNAc residue at the released product. These enzymes are involved in the cleavage of the septum
during cell division.
Peptidoglycan hydrolase activity of MltC was demonstrated |CITS: [9158737]|.
A mutant containing deletions in mltC, mltD, and mltE has a defect in cell separation, growing as
short chains of cells |CITS: [12399477]|. These chain-forming mutants have a defect in the barrier function of the
outer membrane. A mutant strain lacking all six known lytic transglycosylases (mltA mltB mltC mltD mltE slt) is
unable to induce β-lactamase and is more susceptible to certain high-molecular weight antibiotics which are
normally inactive against Gram-negative bacteria, such as bacitracin, gallidermin and vancomycin |CITS: [15793119]|.
Expression of mltC is induced by oxidative stress via SoxS |CITS: [14594836]|.
Review: |CITS: [7487333]|)""",
('B4392', 'MLTGY3pp') : """(Slt70 is involved in growth and recycling of peptidoglycan by catalyzing
the lysis of the β-1,4 glycosidic bond between N-acetylmuramic
acid and N-acetylglucosamine, producing 1,6-anhydromuropeptides at
an optimal pH of 4.5 with a Km of 200 mg/L |CITS:[357]|.
Slt70 forms a murein-metabolizing multi-enzyme complex with PBP3 and
PBP7/8 |CITS:[8063800]|. PBP7/8 was shown to stabilize and stimulate the
activity of Slt70 |CITS:[8063800]|. Slt70 activity is also modulated by the
stringent response |CITS:[1970319]|.
The structure of Slt70 has been determined by X-ray crystallography
revealing a α-superhelix structure with the catalytic domain on
top |CITS:[2184239],[8107871]|. The structure has also been determined
to a resolution of 1.65 Å for its native form, 1.90 Å as a
complex with 1,6-anhydromuropeptide |CITS:[10452894]|, and 2.8 Å
as a complex with bulgecin A |CITS:[7548026]|, its inhibitor |CITS:[1400320]|.
Overproduction of Slt70 resulted in growth inhibition and lysis of some cells,
but a deletion mutant had no observable phenotype |CITS:[1938883]|.
Review: |CITS:[9529891]|
)""",
('B2813', 'MLTGY3pp') : """(MltA is one of three (along with MltB and Slt70) major lytic endotransglycosylases expressed in Escherichia coli.
MltA and MltB are expressed as membrane-bound lipoproteins. Overexpression of MltA resulted in elevated levels of
a membrane fraction protein with a molecular mass corresponding to the mass of the purified MltA protein |CITS:[8288527]|.
Expression of MltA in cells grown in the presence of H-3 palmitate followed by SDS-PAGE analysis resulted in
fluorographic visualization of a labeled band corresponding to the 39 kDa mass of MltA, demonstrating the lipoprotein
character of MltA |CITS:[6988430]|. Sucrose gradient centrifugation studies have shown that MltA is localized to the
outer membrane |CITS:[9287002]|. Induced overexpression of MltA resulted in lysis of cells grown at 30 degrees Celsius,
the optimal temperature for enzymatic activity, but not at 37 degrees. Furthermore the expressed activity was able to
hydrolyze both murein sacculi as well as isolated glycan strands |CITS:[9287002]|. A triple mltA, mltB, and
slt70 mutant resulted in a 72% reduction in murein turnover |CITS:[10572120]|.)""",
('B2701', 'MLTGY3pp') : """(MltB is one of three (along with MltA and Slt70) major lytic endotransglycosylases expressed in
Escherichia coli. MltA and MltB are expressed as membrane-bound lipoproteins. Expression
of MltB in cells grown in the presence of H-3 palmitate followed by SDS-PAGE analysis resulted in
fluorographic visualization of a labeled band corresponding to the 36 kDa mass of MltB, demonstrating
the lipoprotein character of MltB. Additionally, in the presence of globomycin, an inhibitor of the
lipoprotein signal peptidase, a larger protein, the prolipoprotein form of MltB, was found to accumulate.
Overexpression of mltB resulted in a 55-fold increase in murein hydrolase activity in the membrane
fraction and subsequent cell lysis. Membrane fractionation followed by sucrose-density-gradient
centrifugation indicated that most of the induced hydrolytic activity was located in the outer and
intermediate membrane fractions. A deletion of the mltB gene showed no obvious phenotype
|CITS:[746170]|, while a triple mltA, mltB, and slt70 mutant resulted in a 72%
reduction in murein turnover |CITS:[10572120]|.)""",
('B2835', '2AGPG181tipp') : """(LplT is a major facilitator superfamily (MFS) protein that acts as a flippase for transbilayer movement of
lysophospholipids. Mutation experiments and
transporter assays have determined LplT is responsible for the facilitated diffusion of lysophospholipids to
the cytoplasmic portion of the inner membrane providing substrate for the bifunctional enzyme
2-acyl-GPE acyltransferase/acyl-ACP synthetase (Aas). lplT forms an operon with the aas
gene |CITS:[15661733]|.)""",
('B2492', 'FORt2pp') : """(FocB is a putative formate transporter, belonging to the FNT
family of formate and nitrite transporters |CITS: [99184734]|.
The focB gene is located in the putative twelve gene hyf
operon, which includes nine genes encoding a putative formate
hydrogenlyase complex |CITS: [98048487]|. FocB is highly similar
to the formate transporter FocA, and presumably functions as a
formate transporter reponsible for uptake of formate to provide
a substrate for the formate hydrogenlyase.)""",
('B3803', 'UPP3MT') : """(The HemX protein was suggested to be a uroporphyrinogen III methylase |CITS: [3062586]|. However, the function
of the protein has not been experimentally determined.
HemX exists as a homooligomer in the inner membrane |CITS: [16079137]|.)""",
('B3793', 'ECAP3pp') : """(wzyE has been proposed to encode the polymerase involved in the assembly of linear ECA polysaccharide
chains |CITS: [11673418][12618464][12621029]|. A wzyE null mutant was reported to be unable to synthesize
ECA and to accumulate lipid III |CITS: [11673418]|.
A larger open reading frame in this region was originally thought to exist and encode the
4-alpha-L-fucosyltransferase, which is in fact encoded by the gene directly upstream of wzyE, rffT
|CITS: [11673418]|.)""",
('B3793', 'ECAP3pp') : """(The Enterobacterial Common Antigen biosynthesis protein complex is responsible for synthesizing ECA
polysaccharide chains from Lipid III precursors that have been transferred accross the inner membrane.)""",
('B3785', 'ECAP3pp') : """(WzzE is responsible for regulating the length of phosphoglyceride-linked
Enterobacterial Common Antigen (ECAPG) polysaccharide
chains formed from polymerization by WzyE utilizing Lipid III in the periplasm.
Typically, ECAPG chain lengths are 1 to 14 repeats long with
a modal value of 6 or 7. wzzE mutants display a random, non-modal
distribution of ECAPG polysaccharide chain lengths |CITS:[10515954]|.
wzzE has been shown to be required for the synthesis of cyclic ECA
which contains 4 trisaccharide repeat units and is located in the periplasm
|CITS:[16199561]|. WzzE is predicted to form a complex with WzyE and WzxE
|CITS:[16816184]|.)""",
('B3785', 'ECAP3pp') : """(The Enterobacterial Common Antigen biosynthesis protein complex is responsible for synthesizing ECA
polysaccharide chains from Lipid III precursors that have been transferred accross the inner membrane.)""",
('B0936', 'ETHSO3abcpp') : """NIL""",
('B0936', 'ETHSO3abcpp') : """(Deletion mutation studies |CITS:[10506196]| indicate that the ssuEADCB gene cluster codes for proteins that enable Escherichia coli
to utilize sulfonates other than taurine as a sulfur source. Based on sequence similarity SsuABC is the ABC type transport system with
SsuA being the periplasmic substrate-binding subunit, SsuB the ATP-binding subunit and SsuC the permease. ssuD and
ssuE encode an FMNH2-dependent monooxygenase and an NAD(P)H-dependent FMN reductase, respectively.)""",
('B0933', 'ETHSO3abcpp') : """(ATP-binding component of ABC transporter)""",
('B0933', 'ETHSO3abcpp') : """(Deletion mutation studies |CITS:[10506196]| indicate that the ssuEADCB gene cluster codes for proteins that enable Escherichia coli
to utilize sulfonates other than taurine as a sulfur source. Based on sequence similarity SsuABC is the ABC type transport system with
SsuA being the periplasmic substrate-binding subunit, SsuB the ATP-binding subunit and SsuC the permease. ssuD and
ssuE encode an FMNH2-dependent monooxygenase and an NAD(P)H-dependent FMN reductase, respectively.)""",
('B0934', 'ETHSO3abcpp') : """(membrane component of ABC transporter
Protein topology in the inner membrane has been determined |CITS: [11867724]|.)""",
('B0934', 'ETHSO3abcpp') : """(Deletion mutation studies |CITS:[10506196]| indicate that the ssuEADCB gene cluster codes for proteins that enable Escherichia coli
to utilize sulfonates other than taurine as a sulfur source. Based on sequence similarity SsuABC is the ABC type transport system with
SsuA being the periplasmic substrate-binding subunit, SsuB the ATP-binding subunit and SsuC the permease. ssuD and
ssuE encode an FMNH2-dependent monooxygenase and an NAD(P)H-dependent FMN reductase, respectively.)""",
('B1466', 'NO3R2pp') : """(The polypeptide encoded by narW, the third gene in the narZYWV operon, is not part of the final
nitrate reductase Z enzyme. By similarity to NarJ, it may act as a private chaperone during the incorporation of the
molybdenum cofactor into NarZ, the α subunit of nitrate reductase Z |CITS: [92186712]|.
)""",
('B1226', 'NO3R2pp') : """(NarJ is parto of the redox enzyme maturation protein (REMP) family of chaperones |CITS: [15213747]|. NarJ acts as
a private chaperone during the incorporation of the molybdenum cofactor into NarG, the α subunit of nitrate
reductase A |CITS: [8793883][9305880][9632249][15247236]|.
NarJ, encoded by the third gene in the narGHJI operon, is not part of the final nitrate reductase A enzyme, but
is essential for nitrate reductase activity |CITS: [3053688][92186712][1732220]|. NarJ interacts with the NarG subunit
of the apoenzyme complex at two distinct sites. One site is located at the N terminus of NarG and interferes with
membrane anchoring of the complex |CITS: [16286471][16540088]|, while the second site is involved in the insertion
of the molybdenum cofactor, which precedes membrane anchoring |CITS: [16286471]|. Thus, NarJ appears to
coordinate the final assembly and cofactor acquisition of nitrate reductase A.
Review: |CITS: [15213747]|)""",
('B2835', '2AGPE181tipp') : """(LplT is a major facilitator superfamily (MFS) protein that acts as a flippase for transbilayer movement of
lysophospholipids. Mutation experiments and
transporter assays have determined LplT is responsible for the facilitated diffusion of lysophospholipids to
the cytoplasmic portion of the inner membrane providing substrate for the bifunctional enzyme
2-acyl-GPE acyltransferase/acyl-ACP synthetase (Aas). lplT forms an operon with the aas
gene |CITS:[15661733]|.)""",
('B0411', 'GUAtex') : """(Tsx is a protein involved with the permeation of ribo- and deoxy-nucleosides, across the outer membrane of E. coli.
It also allows the entry of the antibiotic albicidin, and serves as a receptor for bacteriophage and colicins |CITS: [3276691]|
It is believed to form a 14 strand β-barrel porin.
The crystal structure of Tsx has been determined up to 3.1 A co-crystallized with a range of nucleosides |CITS:[15272310]|. Tsx has been shown to localize to the cellular poles |CITS:[15130122]|.)""",
('B3290', 'Kt2pp') : """(trkA mutants were identified in a kdp background as
requiring significantly elevated levels of K+ for growth
|CITS:[4942756]|. trkA encodes part of a K+
transport system |CITS:[4942756]|. The TrkA system is constitutive
with a Km of 1.5 mM |CITS:[4578]|. K+ uptake by TrkA
is both ATP-dependent and protonmotive force (pmf)-driven |CITS:[320207]|,
though K+ exchange is not dependent upon the pmf
|CITS:[359759]|. TrkA is inhibited by high intracellular K+
|CITS:[359759]| and by low pH |CITS:[6405784]|. Efflux of K+
by TrkA depends upon the intracellular concentration of K+
|CITS:[7042336]|. trkE, trkG, and trkH mutations reduced
or prevented binding of TrkA to the membrane |CITS:[2674131]|.
The TrkG and TrkH membrane proteins were identified as two different
but nearly equivalent systems of K+ uptake, each requiring
TrkA and TrkE |CITS:[1987159]|. UV crosslinking studies showed binding
of TrkA to NAD+ but not to ATP |CITS:[8412700]|. The TrkA pump may
be involved in regulation of pH in anaerobically growing cells at alkaline
pH |CITS:[9829260]|. The F0F1 ATPase is
dependent on TrkA when cells are grown anaerobically on glucose at
alkaline pH |CITS:[12804571]|.)""",
('B3290', 'Kt2pp') : """(trkA mutants were identified in a kdp background as
requiring significantly elevated levels of K+ for growth
|CITS:[4942756]|. trkA encodes part of a K+
transport system |CITS:[4942756]|. The TrkA system is constitutive
with a Km of 1.5 mM |CITS:[4578]|. K+ uptake by TrkA
is both ATP-dependent and protonmotive force (pmf)-driven |CITS:[320207]|,
though K+ exchange is not dependent upon the pmf
|CITS:[359759]|. TrkA is inhibited by high intracellular K+
|CITS:[359759]| and by low pH |CITS:[6405784]|. Efflux of K+
by TrkA depends upon the intracellular concentration of K+
|CITS:[7042336]|. trkE, trkG, and trkH mutations reduced
or prevented binding of TrkA to the membrane |CITS:[2674131]|.
The TrkG and TrkH membrane proteins were identified as two different
but nearly equivalent systems of K+ uptake, each requiring
TrkA and TrkE |CITS:[1987159]|. UV crosslinking studies showed binding
of TrkA to NAD+ but not to ATP |CITS:[8412700]|. The TrkA pump may
be involved in regulation of pH in anaerobically growing cells at alkaline
pH |CITS:[9829260]|. The F0F1 ATPase is
dependent on TrkA when cells are grown anaerobically on glucose at
alkaline pH |CITS:[12804571]|.)""",
('B1487', 'ALAALAabcpp') : """(periplasmic binding component of ABC transporter)""",
('B1487', 'ALAALAabcpp') : """(YddO, YddP, YddQ, YddR and YddS are uncharacterized
members of the ABC superfamily of transporters |CITS: [99091701]|.
YddO and YddP are the putative ATP-binding proteins.
YddQ and YddR are the putative membrane components.
YddS is the putativeperiplasmic binding protein.
Based on sequence similarity, these proteins probably
function together as an ATP-dependent peptide transporter.
The genes yddO, yddP, yddQ, yddR,
and yddS are probably located within a single
operon.)""",
('B1486', 'ALAALAabcpp') : """(membrane component of ABC transporter)""",
('B1486', 'ALAALAabcpp') : """(YddO, YddP, YddQ, YddR and YddS are uncharacterized
members of the ABC superfamily of transporters |CITS: [99091701]|.
YddO and YddP are the putative ATP-binding proteins.
YddQ and YddR are the putative membrane components.
YddS is the putativeperiplasmic binding protein.
Based on sequence similarity, these proteins probably
function together as an ATP-dependent peptide transporter.
The genes yddO, yddP, yddQ, yddR,
and yddS are probably located within a single
operon.)""",
('B1485', 'ALAALAabcpp') : """(membrane component of ABC transporter
Protein topology in the inner membrane has been determined |CITS: [11867724]|.)""",
('B1485', 'ALAALAabcpp') : """(YddO, YddP, YddQ, YddR and YddS are uncharacterized
members of the ABC superfamily of transporters |CITS: [99091701]|.
YddO and YddP are the putative ATP-binding proteins.
YddQ and YddR are the putative membrane components.
YddS is the putativeperiplasmic binding protein.
Based on sequence similarity, these proteins probably
function together as an ATP-dependent peptide transporter.
The genes yddO, yddP, yddQ, yddR,
and yddS are probably located within a single
operon.)""",
('B1484', 'ALAALAabcpp') : """(ATP-binding component of ABC transporter)""",
('B1484', 'ALAALAabcpp') : """(YddO, YddP, YddQ, YddR and YddS are uncharacterized
members of the ABC superfamily of transporters |CITS: [99091701]|.
YddO and YddP are the putative ATP-binding proteins.
YddQ and YddR are the putative membrane components.
YddS is the putativeperiplasmic binding protein.
Based on sequence similarity, these proteins probably
function together as an ATP-dependent peptide transporter.
The genes yddO, yddP, yddQ, yddR,
and yddS are probably located within a single
operon.)""",
('B1483', 'ALAALAabcpp') : """(ATP-binding component of ABC transporter)""",
('B1483', 'ALAALAabcpp') : """(YddO, YddP, YddQ, YddR and YddS are uncharacterized
members of the ABC superfamily of transporters |CITS: [99091701]|.
YddO and YddP are the putative ATP-binding proteins.
YddQ and YddR are the putative membrane components.
YddS is the putativeperiplasmic binding protein.
Based on sequence similarity, these proteins probably
function together as an ATP-dependent peptide transporter.
The genes yddO, yddP, yddQ, yddR,
and yddS are probably located within a single
operon.)""",
('B0411', 'DCYTtex') : """(Tsx is a protein involved with the permeation of ribo- and deoxy-nucleosides, across the outer membrane of E. coli.
It also allows the entry of the antibiotic albicidin, and serves as a receptor for bacteriophage and colicins |CITS: [3276691]|
It is believed to form a 14 strand β-barrel porin.
The crystal structure of Tsx has been determined up to 3.1 A co-crystallized with a range of nucleosides |CITS:[15272310]|. Tsx has been shown to localize to the cellular poles |CITS:[15130122]|.)""",
('B2835', '2AGPE120tipp') : """(LplT is a major facilitator superfamily (MFS) protein that acts as a flippase for transbilayer movement of
lysophospholipids. Mutation experiments and
transporter assays have determined LplT is responsible for the facilitated diffusion of lysophospholipids to
the cytoplasmic portion of the inner membrane providing substrate for the bifunctional enzyme
2-acyl-GPE acyltransferase/acyl-ACP synthetase (Aas). lplT forms an operon with the aas
gene |CITS:[15661733]|.)""",
('B2835', '2AGPA161tipp') : """(LplT is a major facilitator superfamily (MFS) protein that acts as a flippase for transbilayer movement of
lysophospholipids. Mutation experiments and
transporter assays have determined LplT is responsible for the facilitated diffusion of lysophospholipids to
the cytoplasmic portion of the inner membrane providing substrate for the bifunctional enzyme
2-acyl-GPE acyltransferase/acyl-ACP synthetase (Aas). lplT forms an operon with the aas
gene |CITS:[15661733]|.)""",
('B2523', 'AMPTASEPG') : """(The pepB gene encodes an aminopeptidase (AP) |CITS: [372108]|.)""",
('B1801', 'GLYBt2pp') : """(YeaV is an uncharacterized member of the Betaine, Carnitine, Choline Transporter (BCCT)
family |CITS:[95115548]|. Based on bioinformatic analysis, YeaV shows highest amino acid sequence
similarity with carnitine transporters.)""",
('B2490', 'FHL') : """(The hyfJ gene is part of the hyf operon, and expression of adjacent genes may be translationally coupled
|CITS: [12426353]|. The HyfJ protein is similar to HycH, the formate hydrogenlyase maturation protein responsible
for processing of the large subunit (HycE) of hydrogenase 3.)""",
('B1296', 'PTRCt2pp') : """(The YcjJ protein is a member of the
APC superfamily of amino acid transporters.
Based on sequence similarity, YcjJ may function as a proton-driven
amino acid uptake system.
PuuP is a putrescine importer |CITS: [15590624]|.)""",
('B0084', 'MCTP2App') : """(FtsI (penicillin-binding protein 3, PBP3) is an essential cell division protein |CITS: [1103132]| which is present at low
abundance of about 100 molecules per cell |CITS: [9379897]|. Binding of beta-lactam antibiotics to FtsI inhibits FtsI
activity and is lethal |CITS: [3902760]|. FtsI is localized to the division site; localization is dependent on FtsZ, FtsA,
FtsQ, FtsL, and FtsW, but not FtsN |CITS: [9379897][9603865][9882665][11703663][11807049]|. FtsA alone can
force FtsI to localize to the cell poles independently of the Z ring, suggesting that FtsA and FtsI interact in a separate
pathway |CITS: [15516588]|. This is supported by bacterial two-hybrid evidence |CITS: [14663069]|.
FtsI contains a small N-terminal cytoplasmic domain, a transmembrane helix and a C-terminal periplasmic region that
can be separated into a noncatalytic and a catalytic domain |CITS: [2677607][9614966]|. The cytoplasmic domain
and transmembrane helix are essential for its role in cell division |CITS: [9260951][8631709]|. The transmembrane
helix is necessary and sufficient for localization of FtsI to the Z ring |CITS: [9882665][14702319][15601716]|. The
noncatalytic periplasmic domain is required for recruitment of FtsN |CITS: [14702319]|. The catalytic C-terminal
domain contains the transpeptidase activity and is involved in peptidoglycan synthesis at the division septum
|CITS: [6450748][3531167][9260951]|. Constriction of the Z ring during cell division requires the transpeptidase
activity of FtsI |CITS: [9012823]|. The C-terminal 349 amino acids contain the penicillin-binding region
|CITS: [6092133]|. A fraction of FtsI molecules are modified with glycerol and fatty acids |CITS: [3053665]|.
Overproduction of FtsI suppresses the filamentous phenotype of strains with mutations in ftsI and ftsH
|CITS: [3316193]|.
Inactivation of FtsI by binding of beta-lactam antibiotics or mutagenesis induces the SOS response via the DpiBA
two-component signal transduction system. The resulting cell division arrest may enable survival of the cells despite
exposure to otherwise lethal antibiotics |CITS: [15308764]|.
Selected reviews: |CITS: [15491352][12626683][9614966]|)""",
('B0635', 'MCTP2App') : """(The mrdA (or pbpA) gene encodes the PBP2 protein responsible for maintaining the rod cell shape and mecillinam sensitivity in E. coli along with rodA |CITS:[6243629]|, |CITS:[1091862]|. The pbpA and rodA genes are members of a single transcriptional unit called the rodA operon, and rodA also has its own promoter within the pbpA gene |CITS:[2644207]|, |CITS:[6300030]|. Biochemical assays have shown that PBP2 is probably a bifunctional enzyme involved in the formation and cross-linking of peptidoglycan by transglycosylation and transpeptidation |CITS:[3009484]|. The active site was identified by the SXXK box at serine 330 |CITS:[3533535]|. The transpeptidase activity and penicillin-binding property of PBP2 are separable |CITS:[2656638]|. PBP2 exists at an estimated 10 to 20 copies per cell |CITS:[319999]|. The pbpA gene has been found to be deleterious for growth at high copy number |CITS:[6348028]|. PBP2 has no signal peptide, and a stretch of 25 non-ionic amino acids in the N-terminal region anchors the protein in the inner membrane |CITS:[3533535]|. GFP-PBP2 fusions have been shown to localize in the cylindrical portion of the cell membrane as well as at the site of constriction prior to division, but not in the old pole. The signal at the site of constriction disappears just before separation of daughter cells. This localization at mid-cell was dependent upon active PBP3, though PBP2 was found to not be a stable component of the divisome. PBP2 is active at the division site and required to maintain the diameter of the newly formed pole there |CITS:[12519203]|.
Mutation or inhibition of PBP2 alone or coupled with mutation or inhibition of other proteins involved in murein synthesis or cell division have been isolated and characterized. |CITS:[345275]|, |CITS:[201607]|, |CITS:[363690]|, |CITS:[6243629]|, |CITS:[6451612]|, |CITS:[7007327]|, |CITS:[7027927]|, |CITS:[3894330]|, |CITS:[2066344]|, |CITS:[8407846]|, |CITS:[2656638]|, |CITS:[1038366]|, |CITS:[1103132]|, |CITS:[11418550]|.
Buoyant density studies of pbpA mutants have been performed |CITS:[1885519]|.
)""",
('B3396', 'MCTP2App') : """(PBP1A is the product of the mrcA gene |CITS:[3882429]|. PBP1A is a bifunctional, inner membrane enzyme
catalyzing the transglycosylation and transpeptidation of murein (peptidoglycan) precursors in the formation of the
murein sacculus |CITS:[9529891]|. The amino terminus contains a signal sequence |CITS:[3882429]|. PBP1A is able
to dimerize without disulfide bonds, but doesn't form a complex with PBP1B |CITS:[12057973]|. Either PBP1A or
PBP1B (the other major bifunctional enzyme in murein synthesis with a different penicillin-binding affinity) is required
for cell elongation because a PBP1A-PBP1B double mutation is lethal |CITS:[1103132][341159][345275][2993822]|.
Experiments have been performed involving inhibition or mutation of PBP1A alone or coupled with inhibition or
mutation of other proteins involved in cell division and murein metabolism |CITS:[7007327][2211517][2066344][10383966]|.)""",
('B2835', '2AGPA120tipp') : """(LplT is a major facilitator superfamily (MFS) protein that acts as a flippase for transbilayer movement of
lysophospholipids. Mutation experiments and
transporter assays have determined LplT is responsible for the facilitated diffusion of lysophospholipids to
the cytoplasmic portion of the inner membrane providing substrate for the bifunctional enzyme
2-acyl-GPE acyltransferase/acyl-ACP synthetase (Aas). lplT forms an operon with the aas
gene |CITS:[15661733]|.)""",
('B3781', 'TRDR') : """(Thioredoxin is a small electron-transfer protein which contains a cysteine
disulfide/dithiol active site. The protein functions in a wide variety of cellular
processes. Thioredoxin is reduced by NADPH in a reaction catalyzed by
thioredoxin reductase. The conversion between the oxidized and reduced
forms results in a change of conformation. The functional properties differ
between the two forms of thioredoxin. The reduced thioredoxin is a powerful
protein disulfide reductase, thioredoxin catalyzes dithiol-disulfide exchange
reactions. The oxidized form of thioredoxin has been crystallized,
the reduced form has been solved by NMR. |CITS: [85277988] [90198521]
[90254096] [90298180] [93264420] [90204538]|)""",
('B3781', 'TRDR') : """(Thioredoxin is a small electron-transfer protein which contains a cysteine
disulfide/dithiol active site. The protein functions in a wide variety of cellular
processes. Thioredoxin is reduced by NADPH in a reaction catalyzed by
thioredoxin reductase. The conversion between the oxidized and reduced
forms results in a change of conformation. The functional properties differ
between the two forms of thioredoxin. The reduced thioredoxin is a powerful
protein disulfide reductase, thioredoxin catalyzes dithiol-disulfide exchange
reactions. The oxidized form of thioredoxin has been crystallized, the reduced
form has been solved by NMR.
|CITS: [85277988] [90198521] [90254096] [90298180] [93264420] [90204538]|)""",
('B2582', 'TRDR') : """(The trxC gene encodes a second thioredoxin in E. coli. Thioredoxin 2 can perform many of
thioredoxin 1's roles in vivo; it is able to reduce some essential cytoplasmic enzymes.
Along with thioredoxin 1 and glutaredoxin 1, thioredoxin 2 is one of E. coli's most
effective cytoplasmic disulfide-reducing proteins. Any one of these three is sufficient
to support aerobic growth. |CITS: [98429478] [98049550]|)""",
('B2582', 'TRDR') : """NIL""",
('B2835', '2AGPG180tipp') : """(LplT is a major facilitator superfamily (MFS) protein that acts as a flippase for transbilayer movement of
lysophospholipids. Mutation experiments and
transporter assays have determined LplT is responsible for the facilitated diffusion of lysophospholipids to
the cytoplasmic portion of the inner membrane providing substrate for the bifunctional enzyme
2-acyl-GPE acyltransferase/acyl-ACP synthetase (Aas). lplT forms an operon with the aas
gene |CITS:[15661733]|.)""",
('B2035', 'O16AP1pp') : """(Lipopolysaccharide (LPS) is a major component of the outer membrane in most gram-negative
bacteria. It consists of lipid A, core oligosaccharide, and O polysaccharide or O-specific antigen.
E. coli K-12 does not normally express O-specific LPS due to mutations in its laterally acquired
rfb gene cluster. rfc is found within the rfb gene cluster and encodes an O-antigen
polymerase |CITS:[7517390],[7517391]|. When the rfb-50 mutation of W3110 is complemented
with the rfb cluster from strain WG1, O16 O antigen is synthesized |CITS:[7517391]|.)""",
('B2027', 'O16AP1pp') : """(In E. coli strains O8 and O9, the orthologous Wzz protein was shown to control the length of the O-antigen
component of lipopolysaccharide |CITS: [8606163][9383197]|. Regulation of O-antigen chain length is required
for virulence of Salmonella typhimurium |CITS: [12603743]|. E. coli K12 does not produce O-antigen.
WzzB appears to be present as a dimer in the membrane |CITS: [16079137]|.
rol: "regulator of O length" |CITS: [1715860]|
cld: "chain length determinant" |CITS: [7682279]|)""",
('B1006', 'URAt2rpp') : """(E. coli K-12 contains a previously undescribed pathway for pyrimidine degradation. The enzymes of the
pathway are encoded by the rutABCDEFG operon. The rutG gene product is an uncharacterized
member of the NCS2 family of nucleobase transporters. Based on sequence similarity, RutG may function as a
proton-driven uracil uptake system.
RutG contains 11 predicted transmembrane helices; the C terminus of the protein is located on the cytoplasmic side
of the inner membrane |CITS: [15919996]|.
The rutG gene is the last gene in an operon together with genes involved in the utilization of
pyrimidines as nitrogen sources. Expression of the rutABCDEFG operon is under the control of nitrogen
regulatory protein C (NtrC) |CITS: [11121068]|.
RutG: "pyrimidine utilization" |CITS: [16540542]|
)""",
('B3793', 'ECAP1pp') : """(wzyE has been proposed to encode the polymerase involved in the assembly of linear ECA polysaccharide
chains |CITS: [11673418][12618464][12621029]|. A wzyE null mutant was reported to be unable to synthesize
ECA and to accumulate lipid III |CITS: [11673418]|.
A larger open reading frame in this region was originally thought to exist and encode the
4-alpha-L-fucosyltransferase, which is in fact encoded by the gene directly upstream of wzyE, rffT
|CITS: [11673418]|.)""",
('B3793', 'ECAP1pp') : """(The Enterobacterial Common Antigen biosynthesis protein complex is responsible for synthesizing ECA
polysaccharide chains from Lipid III precursors that have been transferred accross the inner membrane.)""",
('B3785', 'ECAP1pp') : """(WzzE is responsible for regulating the length of phosphoglyceride-linked
Enterobacterial Common Antigen (ECAPG) polysaccharide
chains formed from polymerization by WzyE utilizing Lipid III in the periplasm.
Typically, ECAPG chain lengths are 1 to 14 repeats long with
a modal value of 6 or 7. wzzE mutants display a random, non-modal
distribution of ECAPG polysaccharide chain lengths |CITS:[10515954]|.
wzzE has been shown to be required for the synthesis of cyclic ECA
which contains 4 trisaccharide repeat units and is located in the periplasm
|CITS:[16199561]|. WzzE is predicted to form a complex with WzyE and WzxE
|CITS:[16816184]|.)""",
('B3785', 'ECAP1pp') : """(The Enterobacterial Common Antigen biosynthesis protein complex is responsible for synthesizing ECA
polysaccharide chains from Lipid III precursors that have been transferred accross the inner membrane.)""",
('B0849', 'RNDR2b') : """NIL""",
('B0849', 'RNDR2b') : """(Glutaredoxins are ubiquitous proteins that catalyze the reduction of disulfides via reduced glutathione (GSH).
Escherichia coli has three glutaredoxins (Grx1, Grx2, and Grx3) containing the classic dithiol active site
CPYC, and a fourth one which contains a monothiol (CGFS) potential active site |CITS: [15833738]|.
The glutaredoxins act as a cofactor enabling intracellular redox reactions through a disulfide/dithiol
enzymatic mechanism involving the active site cysteines. They are used as a
hydrogen donor for the glutathione(GSH)-dependent synthesis of deoxyribonucleotides
by ribonucleotide reductase and reduces specific cysteine residues in
ribonucleotide reductase.
Glutaredoxin are also a hydrogen donor for the reduction of adenosine 3'-phosphate 5'-phosphosulfate
and methionine sulfoxide.
In addition, glutaredoxins also catalyzes GSH-disulfide oxidoreduction reactions with low molecular weight
substrates. |CITS: [79151138] [91242463] [93003075]| There are two additional
glutaredoxins in E. coli whose physiological roles have not been fully
determined. |CITS: [95024051]|)""",
('B3610', 'RNDR2b') : """(There at least three glutaredoxins in E. coli. Glutaredoxin
3 is able to function as a disulfide reductase, but not as well as
glutaredoxin 1. Coupled with cellular glutathione it may be the third
hydrogen donor system in the absence of thioredoxin and glutaredoxin
1. Under normal conditions it is likely that glutaredoxin has other
functions. |CITS: [95024051] [96215095]|)""",
('B3610', 'RNDR2b') : """NIL""",
('B1064', 'RNDR2b') : """(Glutaredoxins are ubiquitous proteins that catalyze the reduction of disulfides via reduced glutathione (GSH).
Escherichia coli has three glutaredoxins (Grx1, Grx2, and Grx3) containing the classic dithiol active site
CPYC, and a fourth one which contains a monothiol (CGFS) potential active site |CITS: [15833738]|.
The glutaredoxins do not act as enzymes, but rather as a cofactor, enabling intracellular redox reactions through
a disulfide/dithiol enzymatic mechanism involving the active site cysteines.
There is almost no similarity between the amino acid sequence of Grx2 (an approximately 27 kDa protein) and Grx1
or Grx3 (both 9-kDa proteins), with the exception of the active site which is identical in all three glutaredoxins.
In contrast to glutaredoxin 1 and 3, Grx 2 is not a hydrogen donor for ribonucleotide reductase.
On the other hand, Grx2 is the primary hydrogen donor to ArsC-catalyzed arsenate reduction (|FRAME: RXN-982|)
|CITS: [10593884]|. It is also the most abundant glutaredoxin in the cell, with an intracellular concentration
of 5 µM, compared with 0.2 µM and 2.4 µM for Grx1 and 3, respectively |CITS: [10593884]|.)""",
('B1064', 'RNDR2b') : """(Glutaredoxins are ubiquitous proteins that catalyze the reduction of disulfides via reduced glutathione (GSH).
Escherichia coli has three glutaredoxins (Grx1, Grx2, and Grx3) containing the classic dithiol active site
CPYC, and a fourth one which contains a monothiol (CGFS) potential active site |CITS: [15833738]|.
The glutaredoxins do not act as enzymes, but rather as a cofactor, enabling intracellular redox reactions through
a disulfide/dithiol enzymatic mechanism involving the active site cysteines.
There is almost no similarity between the amino acid sequence of Grx2 (an approximately 27 kDa protein) and Grx1
or Grx3 (both 9-kDa proteins), with the exception of the active site which is identical in all three glutaredoxins.
In contrast to glutaredoxin 1 and 3, Grx 2 is not a hydrogen donor for ribonucleotide reductase.
On the other hand, Grx2 is the primary hydrogen donor to ArsC-catalyzed arsenate reduction (|FRAME: RXN-982|)
|CITS: [10593884]|. It is also the most abundant glutaredoxin in the cell, with an intracellular concentration
of 5 µM, compared with 0.2 µM and 2.4 µM for Grx1 and 3, respectively |CITS: [10593884]|.)""",
('B1654', 'RNDR2b') : """(Grx4 belongs to the family of monothiol glutaredoxins. Oxidized Grx4 can be reduced by the thioredoxin system or
glutaredoxin 1. Grx4 is not active in the standard glutaredoxin assay |CITS: [15833738]|.
Grx4 is an abundant protein that is upregulated during stationary phase; the increased expression is dependent on
ppGpp |CITS: [15833738]|.
A grxD null mutant could not be obtained |CITS: [15833738]|. grxD has previously been reported to be
essential for aerobic growth in rich media |CITS: [13129938]|.
A solution structure of the reduced form of Grx4 has been determined |CITS: [15840565]|)""",
('B0655', 'GLUabcpp') : """(GltI is the periplasmic-binding component of the GltJKL glutamate ABC transporter |CITS:[10972807],[9593292]|.
gltI was shown to be regulated by the FlhDC flagellar transcriptional regulator |CITS:[15941987]|.
)""",
('B0411', 'INStex') : """(Tsx is a protein involved with the permeation of ribo- and deoxy-nucleosides, across the outer membrane of E. coli.
It also allows the entry of the antibiotic albicidin, and serves as a receptor for bacteriophage and colicins |CITS: [3276691]|
It is believed to form a 14 strand β-barrel porin.
The crystal structure of Tsx has been determined up to 3.1 A co-crystallized with a range of nucleosides |CITS:[15272310]|. Tsx has been shown to localize to the cellular poles |CITS:[15130122]|.)""",
('B2687', 'RHCCE') : """(LuxS is involved in biosynthesis of autoinducer, the hormone-like signal that mediates cell-cell communication during quorum sensing, the response to increased cell density |CITS: [9990077]|. LuxS is the synthase that catalyzes formation of autoinducer 2 (AI-2), which is an acylated homoserine lactone, by cleavage of S-ribosylhomocysteine |CITS: [11489131]|. Recycling of S-adenosylhomocysteine via LuxS-mediated AI-2 formation may have metabolic significance |CITS: [11932438]|.
A luxS mutant exhibits altered expression of 242 genes, compared to wild type |CITS: [11514505]|. A luxS mutant has been examined by large-scale phenotypic assay |CITS: [12897016]|.
The DH5alpha strain has a luxS mutation that prevents autoinducer production, whereas the MG1655 strain produces autoinducer |CITS: [9990077]|.
A crystal structure of Bacillus subtilis LuxS is presented at 1.6 A resolution |CITS: [11553770]|. Bacillus subtilis LuxS is homodimeric |CITS: [11553770]|.
LuxS is involved in regulation of pathogenicity genes in enterohemorrhagic and enteropathogenic E. coli strains |CITS: [10611361], [11489873], [11972776], [12810266], [12847292]|. AI-2 production in an E. coli luxS mutant is functionally complemented by LuxS of Borrelia burgdorferi |CITS: [12117917], [12704164]|, Streptococcus mutans |CITS: [12654815]|, Bacillus anthracis |CITS: [12819077]|, Porphyromonas gingivalis |CITS: [11882711]|, Mannheimia haemolytica A1 |CITS: [11786252]|, Porphyromonas gingivalis |CITS: [11292769]|, Helicobacter pylori |CITS: [10816463]|, Vibrio harveyi |CITS: [9990077]|, or E. coli O157:H7 |CITS: [9990077]|.
Regulation has been described |CITS: [11591692], [12107143]|. Transcription of luxS is induced by acetate |CITS: [11591692]| or by acidic pH |CITS: [12107143]|.
Review: |CITS: [12949525]|.
)""",
('B0260', 'MMETt2pp') : """(MmuP belongs to the APC superfamily of amino acid transporters and is a putative S-methylmethionine transporter
|CITS: [9882684]|.
A mutant with a non-polar in-frame deletion in mmuP is unable to utilize S-methylmethionine as a source of
methionine in a metE metH mutant background |CITS: [9882684]|.
mmuP : "S-methylmethionine utilization" |CITS: [9882684]|)""",
('B2738', 'FCLPA') : """(No information about this protein was found by a literature search conducted on April 25, 2006.)""",
('B2032', 'O16GLCT1') : """(No information about this protein was found by a literature search conducted on November 29, 2005.)""",
('B1801', 'CHLt2pp') : """(YeaV is an uncharacterized member of the Betaine, Carnitine, Choline Transporter (BCCT)
family |CITS:[95115548]|. Based on bioinformatic analysis, YeaV shows highest amino acid sequence
similarity with carnitine transporters.)""",
('B2582', 'DSBDR') : """(The trxC gene encodes a second thioredoxin in E. coli. Thioredoxin 2 can perform many of
thioredoxin 1's roles in vivo; it is able to reduce some essential cytoplasmic enzymes.
Along with thioredoxin 1 and glutaredoxin 1, thioredoxin 2 is one of E. coli's most
effective cytoplasmic disulfide-reducing proteins. Any one of these three is sufficient
to support aerobic growth. |CITS: [98429478] [98049550]|)""",
('B2582', 'DSBDR') : """NIL""",
('B3781', 'DSBDR') : """(Thioredoxin is a small electron-transfer protein which contains a cysteine
disulfide/dithiol active site. The protein functions in a wide variety of cellular
processes. Thioredoxin is reduced by NADPH in a reaction catalyzed by
thioredoxin reductase. The conversion between the oxidized and reduced
forms results in a change of conformation. The functional properties differ
between the two forms of thioredoxin. The reduced thioredoxin is a powerful
protein disulfide reductase, thioredoxin catalyzes dithiol-disulfide exchange
reactions. The oxidized form of thioredoxin has been crystallized,
the reduced form has been solved by NMR. |CITS: [85277988] [90198521]
[90254096] [90298180] [93264420] [90204538]|)""",
('B3781', 'DSBDR') : """(Thioredoxin is a small electron-transfer protein which contains a cysteine
disulfide/dithiol active site. The protein functions in a wide variety of cellular
processes. Thioredoxin is reduced by NADPH in a reaction catalyzed by
thioredoxin reductase. The conversion between the oxidized and reduced
forms results in a change of conformation. The functional properties differ
between the two forms of thioredoxin. The reduced thioredoxin is a powerful
protein disulfide reductase, thioredoxin catalyzes dithiol-disulfide exchange
reactions. The oxidized form of thioredoxin has been crystallized, the reduced
form has been solved by NMR.
|CITS: [85277988] [90198521] [90254096] [90298180] [93264420] [90204538]|)""",
('B0936', 'SULFACabcpp') : """NIL""",
('B0936', 'SULFACabcpp') : """(Deletion mutation studies |CITS:[10506196]| indicate that the ssuEADCB gene cluster codes for proteins that enable Escherichia coli
to utilize sulfonates other than taurine as a sulfur source. Based on sequence similarity SsuABC is the ABC type transport system with
SsuA being the periplasmic substrate-binding subunit, SsuB the ATP-binding subunit and SsuC the permease. ssuD and
ssuE encode an FMNH2-dependent monooxygenase and an NAD(P)H-dependent FMN reductase, respectively.)""",
('B0933', 'SULFACabcpp') : """(ATP-binding component of ABC transporter)""",
('B0933', 'SULFACabcpp') : """(Deletion mutation studies |CITS:[10506196]| indicate that the ssuEADCB gene cluster codes for proteins that enable Escherichia coli
to utilize sulfonates other than taurine as a sulfur source. Based on sequence similarity SsuABC is the ABC type transport system with
SsuA being the periplasmic substrate-binding subunit, SsuB the ATP-binding subunit and SsuC the permease. ssuD and
ssuE encode an FMNH2-dependent monooxygenase and an NAD(P)H-dependent FMN reductase, respectively.)""",
('B0934', 'SULFACabcpp') : """(membrane component of ABC transporter
Protein topology in the inner membrane has been determined |CITS: [11867724]|.)""",
('B0934', 'SULFACabcpp') : """(Deletion mutation studies |CITS:[10506196]| indicate that the ssuEADCB gene cluster codes for proteins that enable Escherichia coli
to utilize sulfonates other than taurine as a sulfur source. Based on sequence similarity SsuABC is the ABC type transport system with
SsuA being the periplasmic substrate-binding subunit, SsuB the ATP-binding subunit and SsuC the permease. ssuD and
ssuE encode an FMNH2-dependent monooxygenase and an NAD(P)H-dependent FMN reductase, respectively.)""",
('B2710', 'NHFRBO') : """NIL""",
('B2710', 'NHFRBO') : """NIL""",
('B2710', 'NHFRBO') : """(Flavorubredoxin (FlRd) is a multidomain protein containing an amino-terminal β-lactamase-like module with a
non-heme di-iron site as the catalytic center, a short chain flavodoxin-like module and a rubredoxin-like
extension. FlRd participates in a reaction that reduces nitric oxide |CITS: [20573621][12101220][11751865]|.
Regulation has been described |CITS: [12529359]|.)""",
('B0849', 'RNDR3b') : """NIL""",
('B0849', 'RNDR3b') : """(Glutaredoxins are ubiquitous proteins that catalyze the reduction of disulfides via reduced glutathione (GSH).
Escherichia coli has three glutaredoxins (Grx1, Grx2, and Grx3) containing the classic dithiol active site
CPYC, and a fourth one which contains a monothiol (CGFS) potential active site |CITS: [15833738]|.
The glutaredoxins act as a cofactor enabling intracellular redox reactions through a disulfide/dithiol
enzymatic mechanism involving the active site cysteines. They are used as a
hydrogen donor for the glutathione(GSH)-dependent synthesis of deoxyribonucleotides
by ribonucleotide reductase and reduces specific cysteine residues in
ribonucleotide reductase.
Glutaredoxin are also a hydrogen donor for the reduction of adenosine 3'-phosphate 5'-phosphosulfate
and methionine sulfoxide.
In addition, glutaredoxins also catalyzes GSH-disulfide oxidoreduction reactions with low molecular weight
substrates. |CITS: [79151138] [91242463] [93003075]| There are two additional
glutaredoxins in E. coli whose physiological roles have not been fully
determined. |CITS: [95024051]|)""",
('B3610', 'RNDR3b') : """(There at least three glutaredoxins in E. coli. Glutaredoxin
3 is able to function as a disulfide reductase, but not as well as
glutaredoxin 1. Coupled with cellular glutathione it may be the third
hydrogen donor system in the absence of thioredoxin and glutaredoxin
1. Under normal conditions it is likely that glutaredoxin has other
functions. |CITS: [95024051] [96215095]|)""",
('B3610', 'RNDR3b') : """NIL""",
('B1654', 'RNDR3b') : """(Grx4 belongs to the family of monothiol glutaredoxins. Oxidized Grx4 can be reduced by the thioredoxin system or
glutaredoxin 1. Grx4 is not active in the standard glutaredoxin assay |CITS: [15833738]|.
Grx4 is an abundant protein that is upregulated during stationary phase; the increased expression is dependent on
ppGpp |CITS: [15833738]|.
A grxD null mutant could not be obtained |CITS: [15833738]|. grxD has previously been reported to be
essential for aerobic growth in rich media |CITS: [13129938]|.
A solution structure of the reduced form of Grx4 has been determined |CITS: [15840565]|)""",
('B1064', 'RNDR3b') : """(Glutaredoxins are ubiquitous proteins that catalyze the reduction of disulfides via reduced glutathione (GSH).
Escherichia coli has three glutaredoxins (Grx1, Grx2, and Grx3) containing the classic dithiol active site
CPYC, and a fourth one which contains a monothiol (CGFS) potential active site |CITS: [15833738]|.
The glutaredoxins do not act as enzymes, but rather as a cofactor, enabling intracellular redox reactions through
a disulfide/dithiol enzymatic mechanism involving the active site cysteines.
There is almost no similarity between the amino acid sequence of Grx2 (an approximately 27 kDa protein) and Grx1
or Grx3 (both 9-kDa proteins), with the exception of the active site which is identical in all three glutaredoxins.
In contrast to glutaredoxin 1 and 3, Grx 2 is not a hydrogen donor for ribonucleotide reductase.
On the other hand, Grx2 is the primary hydrogen donor to ArsC-catalyzed arsenate reduction (|FRAME: RXN-982|)
|CITS: [10593884]|. It is also the most abundant glutaredoxin in the cell, with an intracellular concentration
of 5 µM, compared with 0.2 µM and 2.4 µM for Grx1 and 3, respectively |CITS: [10593884]|.)""",
('B1064', 'RNDR3b') : """(Glutaredoxins are ubiquitous proteins that catalyze the reduction of disulfides via reduced glutathione (GSH).
Escherichia coli has three glutaredoxins (Grx1, Grx2, and Grx3) containing the classic dithiol active site
CPYC, and a fourth one which contains a monothiol (CGFS) potential active site |CITS: [15833738]|.
The glutaredoxins do not act as enzymes, but rather as a cofactor, enabling intracellular redox reactions through
a disulfide/dithiol enzymatic mechanism involving the active site cysteines.
There is almost no similarity between the amino acid sequence of Grx2 (an approximately 27 kDa protein) and Grx1
or Grx3 (both 9-kDa proteins), with the exception of the active site which is identical in all three glutaredoxins.
In contrast to glutaredoxin 1 and 3, Grx 2 is not a hydrogen donor for ribonucleotide reductase.
On the other hand, Grx2 is the primary hydrogen donor to ArsC-catalyzed arsenate reduction (|FRAME: RXN-982|)
|CITS: [10593884]|. It is also the most abundant glutaredoxin in the cell, with an intracellular concentration
of 5 µM, compared with 0.2 µM and 2.4 µM for Grx1 and 3, respectively |CITS: [10593884]|.)""",
('B2033', 'O16AT') : """(No information about this protein was found by a literature search
conducted on February 26, 2004.)""",
('B2835', '2AGPE161tipp') : """(LplT is a major facilitator superfamily (MFS) protein that acts as a flippase for transbilayer movement of
lysophospholipids. Mutation experiments and
transporter assays have determined LplT is responsible for the facilitated diffusion of lysophospholipids to
the cytoplasmic portion of the inner membrane providing substrate for the bifunctional enzyme
2-acyl-GPE acyltransferase/acyl-ACP synthetase (Aas). lplT forms an operon with the aas
gene |CITS:[15661733]|.)""",
('B3622', 'ECA4OALpp') : """(The lipopolysaccharide of E. coli K-12 consists of two major components:
the hydrophobic lipid A moiety inserted into the outer membrane and the
phosphorylated core oligosaccharide |CITS:[12045108]|. E. coli K-12
does not produce O antigen to attach to the LPS core due to a defect in the
rfb gene cluster which can be complemented with genes from a second,
independent rfb mutant to produce an O16 type O antigen |CITS:[7517391]|.
E. coli K-12 may have two major pathways for LPS biosynthesis. One
generates LPS cores suitable for O antigen attachment, and a second generates
lipooligosaccharides (LOS) with modifications to the core structure which prevent
O antigen attachment |CITS:[1385388]|.
WaaL is thought to be the O-antigen ligase in the lipopolysaccharide synthesis pathway.
Unlike most LPS core
biosynthesis genes, waaL has little sequence similarity to the counterpart gene in Salmonella
enterica
|CITS: [1624462]|. This diversity is thought to play a role in generating core specificity and
species-specific
attachment of O antigen |CITS: [1385388]|. WaaL may function together with WaaU |CITS: [9535865]|.
Both WaaU and WaaL are required for the complementation of a waaK mutation in
S. typhimurium LT2, suggesting an interaction between the two proteins |CITS:[1385388]|.
WaaL is an inner membrane protein with 12 predicted membrane-spanning regions. Its C terminus is located in the
cytoplasm |CITS: [15919996]|.
Inactivation of waaL does not cause a detectable
morphological phenotype; this is not surprising, because the
K-12 strain lacks the O antigen |CITS: [1577693]|.
However, waaL appears to be required for core completion
|CITS: [1385388]|. A waaL mutant prevents core completion
by rfp of Shigella dysenteriae 1, suggesting its own
role in core completion |CITS:[1385388]|.
Reviews: |CITS:[12045108],[9157235],[9791168],[7504166]|)""",
('B2035', 'O16AP2pp') : """(Lipopolysaccharide (LPS) is a major component of the outer membrane in most gram-negative
bacteria. It consists of lipid A, core oligosaccharide, and O polysaccharide or O-specific antigen.
E. coli K-12 does not normally express O-specific LPS due to mutations in its laterally acquired
rfb gene cluster. rfc is found within the rfb gene cluster and encodes an O-antigen
polymerase |CITS:[7517390],[7517391]|. When the rfb-50 mutation of W3110 is complemented
with the rfb cluster from strain WG1, O16 O antigen is synthesized |CITS:[7517391]|.)""",
('B2027', 'O16AP2pp') : """(In E. coli strains O8 and O9, the orthologous Wzz protein was shown to control the length of the O-antigen
component of lipopolysaccharide |CITS: [8606163][9383197]|. Regulation of O-antigen chain length is required
for virulence of Salmonella typhimurium |CITS: [12603743]|. E. coli K12 does not produce O-antigen.
WzzB appears to be present as a dimer in the membrane |CITS: [16079137]|.
rol: "regulator of O length" |CITS: [1715860]|
cld: "chain length determinant" |CITS: [7682279]|)""",
('B2835', '2AGPE160tipp') : """(LplT is a major facilitator superfamily (MFS) protein that acts as a flippase for transbilayer movement of
lysophospholipids. Mutation experiments and
transporter assays have determined LplT is responsible for the facilitated diffusion of lysophospholipids to
the cytoplasmic portion of the inner membrane providing substrate for the bifunctional enzyme
2-acyl-GPE acyltransferase/acyl-ACP synthetase (Aas). lplT forms an operon with the aas
gene |CITS:[15661733]|.)""",
('B3469', 'CD2abcpp') : """(The gene product of the yhhO gene, also referred to as zntA, is
a P-type ATPase involved in the efflux of Pb(II), Cd(II), and Zn(II) |CITS:[98070750] [20263730]|.
ZntA displays a Km of approximately 20 μM for Cd(II) and
100 μM for Zn(II) |CITS:[20127859]|. The transporter appears to be inhibited
by vanadate, a common inhibitor of P-type ATPase. The ATPase activity of the
transporter was found to follow the order Pb(II), Cd(II), Zn(II), and Hg(II) |CITS:[20127859]|.
A zntA mutant showed hypersensitivity to Cd(II) and Zn(II) |CITS:[98070750]|.
The zntA gene was found to be under the control of the transcriptional
regulator ZntR. zntA expression is activated by an increased concentration
of Cd(II) and Zn(II) within the cell, showing greater induction by Cd(II) than by
Zn(II) |CITS:[20127859]|.)""",
('B2835', '2AGPG160tipp') : """(LplT is a major facilitator superfamily (MFS) protein that acts as a flippase for transbilayer movement of
lysophospholipids. Mutation experiments and
transporter assays have determined LplT is responsible for the facilitated diffusion of lysophospholipids to
the cytoplasmic portion of the inner membrane providing substrate for the bifunctional enzyme
2-acyl-GPE acyltransferase/acyl-ACP synthetase (Aas). lplT forms an operon with the aas
gene |CITS:[15661733]|.)""",
('B0084', 'MCTP1App') : """(FtsI (penicillin-binding protein 3, PBP3) is an essential cell division protein |CITS: [1103132]| which is present at low
abundance of about 100 molecules per cell |CITS: [9379897]|. Binding of beta-lactam antibiotics to FtsI inhibits FtsI
activity and is lethal |CITS: [3902760]|. FtsI is localized to the division site; localization is dependent on FtsZ, FtsA,
FtsQ, FtsL, and FtsW, but not FtsN |CITS: [9379897][9603865][9882665][11703663][11807049]|. FtsA alone can
force FtsI to localize to the cell poles independently of the Z ring, suggesting that FtsA and FtsI interact in a separate
pathway |CITS: [15516588]|. This is supported by bacterial two-hybrid evidence |CITS: [14663069]|.
FtsI contains a small N-terminal cytoplasmic domain, a transmembrane helix and a C-terminal periplasmic region that
can be separated into a noncatalytic and a catalytic domain |CITS: [2677607][9614966]|. The cytoplasmic domain
and transmembrane helix are essential for its role in cell division |CITS: [9260951][8631709]|. The transmembrane
helix is necessary and sufficient for localization of FtsI to the Z ring |CITS: [9882665][14702319][15601716]|. The
noncatalytic periplasmic domain is required for recruitment of FtsN |CITS: [14702319]|. The catalytic C-terminal
domain contains the transpeptidase activity and is involved in peptidoglycan synthesis at the division septum
|CITS: [6450748][3531167][9260951]|. Constriction of the Z ring during cell division requires the transpeptidase
activity of FtsI |CITS: [9012823]|. The C-terminal 349 amino acids contain the penicillin-binding region
|CITS: [6092133]|. A fraction of FtsI molecules are modified with glycerol and fatty acids |CITS: [3053665]|.
Overproduction of FtsI suppresses the filamentous phenotype of strains with mutations in ftsI and ftsH
|CITS: [3316193]|.
Inactivation of FtsI by binding of beta-lactam antibiotics or mutagenesis induces the SOS response via the DpiBA
two-component signal transduction system. The resulting cell division arrest may enable survival of the cells despite
exposure to otherwise lethal antibiotics |CITS: [15308764]|.
Selected reviews: |CITS: [15491352][12626683][9614966]|)""",
('B0635', 'MCTP1App') : """(The mrdA (or pbpA) gene encodes the PBP2 protein responsible for maintaining the rod cell shape and mecillinam sensitivity in E. coli along with rodA |CITS:[6243629]|, |CITS:[1091862]|. The pbpA and rodA genes are members of a single transcriptional unit called the rodA operon, and rodA also has its own promoter within the pbpA gene |CITS:[2644207]|, |CITS:[6300030]|. Biochemical assays have shown that PBP2 is probably a bifunctional enzyme involved in the formation and cross-linking of peptidoglycan by transglycosylation and transpeptidation |CITS:[3009484]|. The active site was identified by the SXXK box at serine 330 |CITS:[3533535]|. The transpeptidase activity and penicillin-binding property of PBP2 are separable |CITS:[2656638]|. PBP2 exists at an estimated 10 to 20 copies per cell |CITS:[319999]|. The pbpA gene has been found to be deleterious for growth at high copy number |CITS:[6348028]|. PBP2 has no signal peptide, and a stretch of 25 non-ionic amino acids in the N-terminal region anchors the protein in the inner membrane |CITS:[3533535]|. GFP-PBP2 fusions have been shown to localize in the cylindrical portion of the cell membrane as well as at the site of constriction prior to division, but not in the old pole. The signal at the site of constriction disappears just before separation of daughter cells. This localization at mid-cell was dependent upon active PBP3, though PBP2 was found to not be a stable component of the divisome. PBP2 is active at the division site and required to maintain the diameter of the newly formed pole there |CITS:[12519203]|.
Mutation or inhibition of PBP2 alone or coupled with mutation or inhibition of other proteins involved in murein synthesis or cell division have been isolated and characterized. |CITS:[345275]|, |CITS:[201607]|, |CITS:[363690]|, |CITS:[6243629]|, |CITS:[6451612]|, |CITS:[7007327]|, |CITS:[7027927]|, |CITS:[3894330]|, |CITS:[2066344]|, |CITS:[8407846]|, |CITS:[2656638]|, |CITS:[1038366]|, |CITS:[1103132]|, |CITS:[11418550]|.
Buoyant density studies of pbpA mutants have been performed |CITS:[1885519]|.
)""",
('B3396', 'MCTP1App') : """(PBP1A is the product of the mrcA gene |CITS:[3882429]|. PBP1A is a bifunctional, inner membrane enzyme
catalyzing the transglycosylation and transpeptidation of murein (peptidoglycan) precursors in the formation of the
murein sacculus |CITS:[9529891]|. The amino terminus contains a signal sequence |CITS:[3882429]|. PBP1A is able
to dimerize without disulfide bonds, but doesn't form a complex with PBP1B |CITS:[12057973]|. Either PBP1A or
PBP1B (the other major bifunctional enzyme in murein synthesis with a different penicillin-binding affinity) is required
for cell elongation because a PBP1A-PBP1B double mutation is lethal |CITS:[1103132][341159][345275][2993822]|.
Experiments have been performed involving inhibition or mutation of PBP1A alone or coupled with inhibition or
mutation of other proteins involved in cell division and murein metabolism |CITS:[7007327][2211517][2066344][10383966]|.)""",
('B1094', 'UAGAAT') : """(Acyl carrier protein (ACP) plays an important role in fatty
acid biosynthesis. It carries fatty acid chains via a thioester
linkage to a phosphopantetheine prosthetic group as the chains are
elongated. There is also evidence that it has a function in the
biosynthesis of membrane-derived oligosaccharides. Therefore ACP and
its acyl forms interact with at least 12 different E. coli enzymes.
|CITS: [92210530] [89050961] [88296479]| ACP is the most abundant
protein in E. coli, with about 1.5E6 molecules per cell. |CITS: [Mathews&vanHolde]| ACP contains a
phosphopantetheine moiety (as does CoA) as the reactive unit, attached
to the ACP protein through a serine. The holo-ACP synthase enzyme
(encoded by the acpS gene) transfers the 4-phosphopantetheine
moeity of CoA to the apo-ACP to form holo-ACP, which is the active
form of the carrier in lipid synthesis |CITS: [68313114] [81215492]|.)""",
('B1094', 'UAGAAT') : """(Lipoate synthase catalyzes the step of lipoic acid biosynthesis at which sulfur is inserted into octanoyl-ACP to form the lipoate moiety |CITS: [8444795], [11106496]|. Lipoate modification (by lipoyl-protein ligases LipB or LplA) of complex subunits is important for function of pyruvate dehydrogenase |CITS: [814874], [6794598], [8444795]|, alpha-ketoglutarate dehydrogenase |CITS: [814874], [6794598], [8444795]|, and the glycine cleavage system |CITS: [1655709], [8444795]|.)""",
('B1094', 'UAGAAT') : """(Lipoate synthase catalyzes the step of lipoic acid biosynthesis at which sulfur is inserted into octanoyl-ACP to form the lipoate moiety |CITS: [8444795], [11106496]|. Lipoate synthase is a LipA homodimer with two (4Fe-4S) iron-sulfur clusters per protein dimer under anaerobic conditions, and these clusters are oxidized to the (2Fe-2S) state in air |CITS: [10747808], [10403368]|. The enzyme uses octanoyl-ACP, but not octanoic acid, as substrate and also uses S-adenosyl methionine |CITS: [11106496]|.)""",
('B1094', 'UAGAAT') : """NIL""",
('B1094', 'UAGAAT') : """NIL""",
('B1094', 'UAGAAT') : """NIL""",
('B1094', 'UAGAAT') : """NIL""",
('B1094', 'UAGAAT') : """NIL""",
('B1094', 'UAGAAT') : """NIL""",
('B1094', 'UAGAAT') : """NIL""",
('B1094', 'UAGAAT') : """NIL""",
('B1094', 'UAGAAT') : """NIL""",
('B1094', 'UAGAAT') : """NIL""",
('B1094', 'UAGAAT') : """NIL""",
('B1094', 'UAGAAT') : """NIL""",
('B1094', 'UAGAAT') : """NIL""",
('B1094', 'UAGAAT') : """NIL""",
('B1094', 'UAGAAT') : """NIL""",
('B1094', 'UAGAAT') : """NIL""",
('B1094', 'UAGAAT') : """(The holo-ACP synthase enzyme (encoded by acpS) transfers the 4-phosphopantetheine
moiety of CoA to the apo-ACP to form holo-ACP, which is the active
form of the carrier in lipid synthesis |CITS: [68313114] [81215492]|.)""",
('B2523', 'AMPTASECG') : """(The pepB gene encodes an aminopeptidase (AP) |CITS: [372108]|.)""",
('B2035', 'O16AP3pp') : """(Lipopolysaccharide (LPS) is a major component of the outer membrane in most gram-negative
bacteria. It consists of lipid A, core oligosaccharide, and O polysaccharide or O-specific antigen.
E. coli K-12 does not normally express O-specific LPS due to mutations in its laterally acquired
rfb gene cluster. rfc is found within the rfb gene cluster and encodes an O-antigen
polymerase |CITS:[7517390],[7517391]|. When the rfb-50 mutation of W3110 is complemented
with the rfb cluster from strain WG1, O16 O antigen is synthesized |CITS:[7517391]|.)""",
('B2027', 'O16AP3pp') : """(In E. coli strains O8 and O9, the orthologous Wzz protein was shown to control the length of the O-antigen
component of lipopolysaccharide |CITS: [8606163][9383197]|. Regulation of O-antigen chain length is required
for virulence of Salmonella typhimurium |CITS: [12603743]|. E. coli K12 does not produce O-antigen.
WzzB appears to be present as a dimer in the membrane |CITS: [16079137]|.
rol: "regulator of O length" |CITS: [1715860]|
cld: "chain length determinant" |CITS: [7682279]|)""",
('B1094', 'AACPS8') : """(Acyl carrier protein (ACP) plays an important role in fatty
acid biosynthesis. It carries fatty acid chains via a thioester
linkage to a phosphopantetheine prosthetic group as the chains are
elongated. There is also evidence that it has a function in the
biosynthesis of membrane-derived oligosaccharides. Therefore ACP and
its acyl forms interact with at least 12 different E. coli enzymes.
|CITS: [92210530] [89050961] [88296479]| ACP is the most abundant
protein in E. coli, with about 1.5E6 molecules per cell. |CITS: [Mathews&vanHolde]| ACP contains a
phosphopantetheine moiety (as does CoA) as the reactive unit, attached
to the ACP protein through a serine. The holo-ACP synthase enzyme
(encoded by the acpS gene) transfers the 4-phosphopantetheine
moeity of CoA to the apo-ACP to form holo-ACP, which is the active
form of the carrier in lipid synthesis |CITS: [68313114] [81215492]|.)""",
('B1094', 'AACPS8') : """(Lipoate synthase catalyzes the step of lipoic acid biosynthesis at which sulfur is inserted into octanoyl-ACP to form the lipoate moiety |CITS: [8444795], [11106496]|. Lipoate modification (by lipoyl-protein ligases LipB or LplA) of complex subunits is important for function of pyruvate dehydrogenase |CITS: [814874], [6794598], [8444795]|, alpha-ketoglutarate dehydrogenase |CITS: [814874], [6794598], [8444795]|, and the glycine cleavage system |CITS: [1655709], [8444795]|.)""",
('B1094', 'AACPS8') : """(Lipoate synthase catalyzes the step of lipoic acid biosynthesis at which sulfur is inserted into octanoyl-ACP to form the lipoate moiety |CITS: [8444795], [11106496]|. Lipoate synthase is a LipA homodimer with two (4Fe-4S) iron-sulfur clusters per protein dimer under anaerobic conditions, and these clusters are oxidized to the (2Fe-2S) state in air |CITS: [10747808], [10403368]|. The enzyme uses octanoyl-ACP, but not octanoic acid, as substrate and also uses S-adenosyl methionine |CITS: [11106496]|.)""",
('B1094', 'AACPS8') : """NIL""",
('B1094', 'AACPS8') : """NIL""",
('B1094', 'AACPS8') : """NIL""",
('B1094', 'AACPS8') : """NIL""",
('B1094', 'AACPS8') : """NIL""",
('B1094', 'AACPS8') : """NIL""",
('B1094', 'AACPS8') : """NIL""",
('B1094', 'AACPS8') : """NIL""",
('B1094', 'AACPS8') : """NIL""",
('B1094', 'AACPS8') : """NIL""",
('B1094', 'AACPS8') : """NIL""",
('B1094', 'AACPS8') : """NIL""",
('B1094', 'AACPS8') : """NIL""",
('B1094', 'AACPS8') : """NIL""",
('B1094', 'AACPS8') : """NIL""",
('B1094', 'AACPS8') : """NIL""",
('B1094', 'AACPS8') : """(The holo-ACP synthase enzyme (encoded by acpS) transfers the 4-phosphopantetheine
moiety of CoA to the apo-ACP to form holo-ACP, which is the active
form of the carrier in lipid synthesis |CITS: [68313114] [81215492]|.)""",
('B1094', 'AACPS9') : """(Acyl carrier protein (ACP) plays an important role in fatty
acid biosynthesis. It carries fatty acid chains via a thioester
linkage to a phosphopantetheine prosthetic group as the chains are
elongated. There is also evidence that it has a function in the
biosynthesis of membrane-derived oligosaccharides. Therefore ACP and
its acyl forms interact with at least 12 different E. coli enzymes.
|CITS: [92210530] [89050961] [88296479]| ACP is the most abundant
protein in E. coli, with about 1.5E6 molecules per cell. |CITS: [Mathews&vanHolde]| ACP contains a
phosphopantetheine moiety (as does CoA) as the reactive unit, attached
to the ACP protein through a serine. The holo-ACP synthase enzyme
(encoded by the acpS gene) transfers the 4-phosphopantetheine
moeity of CoA to the apo-ACP to form holo-ACP, which is the active
form of the carrier in lipid synthesis |CITS: [68313114] [81215492]|.)""",
('B1094', 'AACPS9') : """(Lipoate synthase catalyzes the step of lipoic acid biosynthesis at which sulfur is inserted into octanoyl-ACP to form the lipoate moiety |CITS: [8444795], [11106496]|. Lipoate modification (by lipoyl-protein ligases LipB or LplA) of complex subunits is important for function of pyruvate dehydrogenase |CITS: [814874], [6794598], [8444795]|, alpha-ketoglutarate dehydrogenase |CITS: [814874], [6794598], [8444795]|, and the glycine cleavage system |CITS: [1655709], [8444795]|.)""",
('B1094', 'AACPS9') : """(Lipoate synthase catalyzes the step of lipoic acid biosynthesis at which sulfur is inserted into octanoyl-ACP to form the lipoate moiety |CITS: [8444795], [11106496]|. Lipoate synthase is a LipA homodimer with two (4Fe-4S) iron-sulfur clusters per protein dimer under anaerobic conditions, and these clusters are oxidized to the (2Fe-2S) state in air |CITS: [10747808], [10403368]|. The enzyme uses octanoyl-ACP, but not octanoic acid, as substrate and also uses S-adenosyl methionine |CITS: [11106496]|.)""",
('B1094', 'AACPS9') : """NIL""",
('B1094', 'AACPS9') : """NIL""",
('B1094', 'AACPS9') : """NIL""",
('B1094', 'AACPS9') : """NIL""",
('B1094', 'AACPS9') : """NIL""",
('B1094', 'AACPS9') : """NIL""",
('B1094', 'AACPS9') : """NIL""",
('B1094', 'AACPS9') : """NIL""",
('B1094', 'AACPS9') : """NIL""",
('B1094', 'AACPS9') : """NIL""",
('B1094', 'AACPS9') : """NIL""",
('B1094', 'AACPS9') : """NIL""",
('B1094', 'AACPS9') : """NIL""",
('B1094', 'AACPS9') : """NIL""",
('B1094', 'AACPS9') : """NIL""",
('B1094', 'AACPS9') : """NIL""",
('B1094', 'AACPS9') : """(The holo-ACP synthase enzyme (encoded by acpS) transfers the 4-phosphopantetheine
moiety of CoA to the apo-ACP to form holo-ACP, which is the active
form of the carrier in lipid synthesis |CITS: [68313114] [81215492]|.)""",
('B1094', 'AACPS4') : """(Acyl carrier protein (ACP) plays an important role in fatty
acid biosynthesis. It carries fatty acid chains via a thioester
linkage to a phosphopantetheine prosthetic group as the chains are
elongated. There is also evidence that it has a function in the
biosynthesis of membrane-derived oligosaccharides. Therefore ACP and
its acyl forms interact with at least 12 different E. coli enzymes.
|CITS: [92210530] [89050961] [88296479]| ACP is the most abundant
protein in E. coli, with about 1.5E6 molecules per cell. |CITS: [Mathews&vanHolde]| ACP contains a
phosphopantetheine moiety (as does CoA) as the reactive unit, attached
to the ACP protein through a serine. The holo-ACP synthase enzyme
(encoded by the acpS gene) transfers the 4-phosphopantetheine
moeity of CoA to the apo-ACP to form holo-ACP, which is the active
form of the carrier in lipid synthesis |CITS: [68313114] [81215492]|.)""",
('B1094', 'AACPS4') : """(Lipoate synthase catalyzes the step of lipoic acid biosynthesis at which sulfur is inserted into octanoyl-ACP to form the lipoate moiety |CITS: [8444795], [11106496]|. Lipoate modification (by lipoyl-protein ligases LipB or LplA) of complex subunits is important for function of pyruvate dehydrogenase |CITS: [814874], [6794598], [8444795]|, alpha-ketoglutarate dehydrogenase |CITS: [814874], [6794598], [8444795]|, and the glycine cleavage system |CITS: [1655709], [8444795]|.)""",
('B1094', 'AACPS4') : """(Lipoate synthase catalyzes the step of lipoic acid biosynthesis at which sulfur is inserted into octanoyl-ACP to form the lipoate moiety |CITS: [8444795], [11106496]|. Lipoate synthase is a LipA homodimer with two (4Fe-4S) iron-sulfur clusters per protein dimer under anaerobic conditions, and these clusters are oxidized to the (2Fe-2S) state in air |CITS: [10747808], [10403368]|. The enzyme uses octanoyl-ACP, but not octanoic acid, as substrate and also uses S-adenosyl methionine |CITS: [11106496]|.)""",
('B1094', 'AACPS4') : """NIL""",
('B1094', 'AACPS4') : """NIL""",
('B1094', 'AACPS4') : """NIL""",
('B1094', 'AACPS4') : """NIL""",
('B1094', 'AACPS4') : """NIL""",
('B1094', 'AACPS4') : """NIL""",
('B1094', 'AACPS4') : """NIL""",
('B1094', 'AACPS4') : """NIL""",
('B1094', 'AACPS4') : """NIL""",
('B1094', 'AACPS4') : """NIL""",
('B1094', 'AACPS4') : """NIL""",
('B1094', 'AACPS4') : """NIL""",
('B1094', 'AACPS4') : """NIL""",
('B1094', 'AACPS4') : """NIL""",
('B1094', 'AACPS4') : """NIL""",
('B1094', 'AACPS4') : """NIL""",
('B1094', 'AACPS4') : """(The holo-ACP synthase enzyme (encoded by acpS) transfers the 4-phosphopantetheine
moiety of CoA to the apo-ACP to form holo-ACP, which is the active
form of the carrier in lipid synthesis |CITS: [68313114] [81215492]|.)""",
('B1094', 'AACPS5') : """(Acyl carrier protein (ACP) plays an important role in fatty
acid biosynthesis. It carries fatty acid chains via a thioester
linkage to a phosphopantetheine prosthetic group as the chains are
elongated. There is also evidence that it has a function in the
biosynthesis of membrane-derived oligosaccharides. Therefore ACP and
its acyl forms interact with at least 12 different E. coli enzymes.
|CITS: [92210530] [89050961] [88296479]| ACP is the most abundant
protein in E. coli, with about 1.5E6 molecules per cell. |CITS: [Mathews&vanHolde]| ACP contains a
phosphopantetheine moiety (as does CoA) as the reactive unit, attached
to the ACP protein through a serine. The holo-ACP synthase enzyme
(encoded by the acpS gene) transfers the 4-phosphopantetheine
moeity of CoA to the apo-ACP to form holo-ACP, which is the active
form of the carrier in lipid synthesis |CITS: [68313114] [81215492]|.)""",
('B1094', 'AACPS5') : """(Lipoate synthase catalyzes the step of lipoic acid biosynthesis at which sulfur is inserted into octanoyl-ACP to form the lipoate moiety |CITS: [8444795], [11106496]|. Lipoate modification (by lipoyl-protein ligases LipB or LplA) of complex subunits is important for function of pyruvate dehydrogenase |CITS: [814874], [6794598], [8444795]|, alpha-ketoglutarate dehydrogenase |CITS: [814874], [6794598], [8444795]|, and the glycine cleavage system |CITS: [1655709], [8444795]|.)""",
('B1094', 'AACPS5') : """(Lipoate synthase catalyzes the step of lipoic acid biosynthesis at which sulfur is inserted into octanoyl-ACP to form the lipoate moiety |CITS: [8444795], [11106496]|. Lipoate synthase is a LipA homodimer with two (4Fe-4S) iron-sulfur clusters per protein dimer under anaerobic conditions, and these clusters are oxidized to the (2Fe-2S) state in air |CITS: [10747808], [10403368]|. The enzyme uses octanoyl-ACP, but not octanoic acid, as substrate and also uses S-adenosyl methionine |CITS: [11106496]|.)""",
('B1094', 'AACPS5') : """NIL""",
('B1094', 'AACPS5') : """NIL""",
('B1094', 'AACPS5') : """NIL""",
('B1094', 'AACPS5') : """NIL""",
('B1094', 'AACPS5') : """NIL""",
('B1094', 'AACPS5') : """NIL""",
('B1094', 'AACPS5') : """NIL""",
('B1094', 'AACPS5') : """NIL""",
('B1094', 'AACPS5') : """NIL""",
('B1094', 'AACPS5') : """NIL""",
('B1094', 'AACPS5') : """NIL""",
('B1094', 'AACPS5') : """NIL""",
('B1094', 'AACPS5') : """NIL""",
('B1094', 'AACPS5') : """NIL""",
('B1094', 'AACPS5') : """NIL""",
('B1094', 'AACPS5') : """NIL""",
('B1094', 'AACPS5') : """(The holo-ACP synthase enzyme (encoded by acpS) transfers the 4-phosphopantetheine
moiety of CoA to the apo-ACP to form holo-ACP, which is the active
form of the carrier in lipid synthesis |CITS: [68313114] [81215492]|.)""",
('B1094', 'AACPS6') : """(Acyl carrier protein (ACP) plays an important role in fatty
acid biosynthesis. It carries fatty acid chains via a thioester
linkage to a phosphopantetheine prosthetic group as the chains are
elongated. There is also evidence that it has a function in the
biosynthesis of membrane-derived oligosaccharides. Therefore ACP and
its acyl forms interact with at least 12 different E. coli enzymes.
|CITS: [92210530] [89050961] [88296479]| ACP is the most abundant
protein in E. coli, with about 1.5E6 molecules per cell. |CITS: [Mathews&vanHolde]| ACP contains a
phosphopantetheine moiety (as does CoA) as the reactive unit, attached
to the ACP protein through a serine. The holo-ACP synthase enzyme
(encoded by the acpS gene) transfers the 4-phosphopantetheine
moeity of CoA to the apo-ACP to form holo-ACP, which is the active
form of the carrier in lipid synthesis |CITS: [68313114] [81215492]|.)""",
('B1094', 'AACPS6') : """(Lipoate synthase catalyzes the step of lipoic acid biosynthesis at which sulfur is inserted into octanoyl-ACP to form the lipoate moiety |CITS: [8444795], [11106496]|. Lipoate modification (by lipoyl-protein ligases LipB or LplA) of complex subunits is important for function of pyruvate dehydrogenase |CITS: [814874], [6794598], [8444795]|, alpha-ketoglutarate dehydrogenase |CITS: [814874], [6794598], [8444795]|, and the glycine cleavage system |CITS: [1655709], [8444795]|.)""",
('B1094', 'AACPS6') : """(Lipoate synthase catalyzes the step of lipoic acid biosynthesis at which sulfur is inserted into octanoyl-ACP to form the lipoate moiety |CITS: [8444795], [11106496]|. Lipoate synthase is a LipA homodimer with two (4Fe-4S) iron-sulfur clusters per protein dimer under anaerobic conditions, and these clusters are oxidized to the (2Fe-2S) state in air |CITS: [10747808], [10403368]|. The enzyme uses octanoyl-ACP, but not octanoic acid, as substrate and also uses S-adenosyl methionine |CITS: [11106496]|.)""",
('B1094', 'AACPS6') : """NIL""",
('B1094', 'AACPS6') : """NIL""",
('B1094', 'AACPS6') : """NIL""",
('B1094', 'AACPS6') : """NIL""",
('B1094', 'AACPS6') : """NIL""",
('B1094', 'AACPS6') : """NIL""",
('B1094', 'AACPS6') : """NIL""",
('B1094', 'AACPS6') : """NIL""",
('B1094', 'AACPS6') : """NIL""",
('B1094', 'AACPS6') : """NIL""",
('B1094', 'AACPS6') : """NIL""",
('B1094', 'AACPS6') : """NIL""",
('B1094', 'AACPS6') : """NIL""",
('B1094', 'AACPS6') : """NIL""",
('B1094', 'AACPS6') : """NIL""",
('B1094', 'AACPS6') : """NIL""",
('B1094', 'AACPS6') : """(The holo-ACP synthase enzyme (encoded by acpS) transfers the 4-phosphopantetheine
moiety of CoA to the apo-ACP to form holo-ACP, which is the active
form of the carrier in lipid synthesis |CITS: [68313114] [81215492]|.)""",
('B1094', 'AACPS7') : """(Acyl carrier protein (ACP) plays an important role in fatty
acid biosynthesis. It carries fatty acid chains via a thioester
linkage to a phosphopantetheine prosthetic group as the chains are
elongated. There is also evidence that it has a function in the
biosynthesis of membrane-derived oligosaccharides. Therefore ACP and
its acyl forms interact with at least 12 different E. coli enzymes.
|CITS: [92210530] [89050961] [88296479]| ACP is the most abundant
protein in E. coli, with about 1.5E6 molecules per cell. |CITS: [Mathews&vanHolde]| ACP contains a
phosphopantetheine moiety (as does CoA) as the reactive unit, attached
to the ACP protein through a serine. The holo-ACP synthase enzyme
(encoded by the acpS gene) transfers the 4-phosphopantetheine
moeity of CoA to the apo-ACP to form holo-ACP, which is the active
form of the carrier in lipid synthesis |CITS: [68313114] [81215492]|.)""",
('B1094', 'AACPS7') : """(Lipoate synthase catalyzes the step of lipoic acid biosynthesis at which sulfur is inserted into octanoyl-ACP to form the lipoate moiety |CITS: [8444795], [11106496]|. Lipoate modification (by lipoyl-protein ligases LipB or LplA) of complex subunits is important for function of pyruvate dehydrogenase |CITS: [814874], [6794598], [8444795]|, alpha-ketoglutarate dehydrogenase |CITS: [814874], [6794598], [8444795]|, and the glycine cleavage system |CITS: [1655709], [8444795]|.)""",
('B1094', 'AACPS7') : """(Lipoate synthase catalyzes the step of lipoic acid biosynthesis at which sulfur is inserted into octanoyl-ACP to form the lipoate moiety |CITS: [8444795], [11106496]|. Lipoate synthase is a LipA homodimer with two (4Fe-4S) iron-sulfur clusters per protein dimer under anaerobic conditions, and these clusters are oxidized to the (2Fe-2S) state in air |CITS: [10747808], [10403368]|. The enzyme uses octanoyl-ACP, but not octanoic acid, as substrate and also uses S-adenosyl methionine |CITS: [11106496]|.)""",
('B1094', 'AACPS7') : """NIL""",
('B1094', 'AACPS7') : """NIL""",
('B1094', 'AACPS7') : """NIL""",
('B1094', 'AACPS7') : """NIL""",
('B1094', 'AACPS7') : """NIL""",
('B1094', 'AACPS7') : """NIL""",
('B1094', 'AACPS7') : """NIL""",
('B1094', 'AACPS7') : """NIL""",
('B1094', 'AACPS7') : """NIL""",
('B1094', 'AACPS7') : """NIL""",
('B1094', 'AACPS7') : """NIL""",
('B1094', 'AACPS7') : """NIL""",
('B1094', 'AACPS7') : """NIL""",
('B1094', 'AACPS7') : """NIL""",
('B1094', 'AACPS7') : """NIL""",
('B1094', 'AACPS7') : """NIL""",
('B1094', 'AACPS7') : """(The holo-ACP synthase enzyme (encoded by acpS) transfers the 4-phosphopantetheine
moiety of CoA to the apo-ACP to form holo-ACP, which is the active
form of the carrier in lipid synthesis |CITS: [68313114] [81215492]|.)""",
('B1094', 'AACPS1') : """(Acyl carrier protein (ACP) plays an important role in fatty
acid biosynthesis. It carries fatty acid chains via a thioester
linkage to a phosphopantetheine prosthetic group as the chains are
elongated. There is also evidence that it has a function in the
biosynthesis of membrane-derived oligosaccharides. Therefore ACP and
its acyl forms interact with at least 12 different E. coli enzymes.
|CITS: [92210530] [89050961] [88296479]| ACP is the most abundant
protein in E. coli, with about 1.5E6 molecules per cell. |CITS: [Mathews&vanHolde]| ACP contains a
phosphopantetheine moiety (as does CoA) as the reactive unit, attached
to the ACP protein through a serine. The holo-ACP synthase enzyme
(encoded by the acpS gene) transfers the 4-phosphopantetheine
moeity of CoA to the apo-ACP to form holo-ACP, which is the active
form of the carrier in lipid synthesis |CITS: [68313114] [81215492]|.)""",
('B1094', 'AACPS1') : """(Lipoate synthase catalyzes the step of lipoic acid biosynthesis at which sulfur is inserted into octanoyl-ACP to form the lipoate moiety |CITS: [8444795], [11106496]|. Lipoate modification (by lipoyl-protein ligases LipB or LplA) of complex subunits is important for function of pyruvate dehydrogenase |CITS: [814874], [6794598], [8444795]|, alpha-ketoglutarate dehydrogenase |CITS: [814874], [6794598], [8444795]|, and the glycine cleavage system |CITS: [1655709], [8444795]|.)""",
('B1094', 'AACPS1') : """(Lipoate synthase catalyzes the step of lipoic acid biosynthesis at which sulfur is inserted into octanoyl-ACP to form the lipoate moiety |CITS: [8444795], [11106496]|. Lipoate synthase is a LipA homodimer with two (4Fe-4S) iron-sulfur clusters per protein dimer under anaerobic conditions, and these clusters are oxidized to the (2Fe-2S) state in air |CITS: [10747808], [10403368]|. The enzyme uses octanoyl-ACP, but not octanoic acid, as substrate and also uses S-adenosyl methionine |CITS: [11106496]|.)""",
('B1094', 'AACPS1') : """NIL""",
('B1094', 'AACPS1') : """NIL""",
('B1094', 'AACPS1') : """NIL""",
('B1094', 'AACPS1') : """NIL""",
('B1094', 'AACPS1') : """NIL""",
('B1094', 'AACPS1') : """NIL""",
('B1094', 'AACPS1') : """NIL""",
('B1094', 'AACPS1') : """NIL""",
('B1094', 'AACPS1') : """NIL""",
('B1094', 'AACPS1') : """NIL""",
('B1094', 'AACPS1') : """NIL""",
('B1094', 'AACPS1') : """NIL""",
('B1094', 'AACPS1') : """NIL""",
('B1094', 'AACPS1') : """NIL""",
('B1094', 'AACPS1') : """NIL""",
('B1094', 'AACPS1') : """NIL""",
('B1094', 'AACPS1') : """(The holo-ACP synthase enzyme (encoded by acpS) transfers the 4-phosphopantetheine
moiety of CoA to the apo-ACP to form holo-ACP, which is the active
form of the carrier in lipid synthesis |CITS: [68313114] [81215492]|.)""",
('B1094', 'AACPS2') : """(Acyl carrier protein (ACP) plays an important role in fatty
acid biosynthesis. It carries fatty acid chains via a thioester
linkage to a phosphopantetheine prosthetic group as the chains are
elongated. There is also evidence that it has a function in the
biosynthesis of membrane-derived oligosaccharides. Therefore ACP and
its acyl forms interact with at least 12 different E. coli enzymes.
|CITS: [92210530] [89050961] [88296479]| ACP is the most abundant
protein in E. coli, with about 1.5E6 molecules per cell. |CITS: [Mathews&vanHolde]| ACP contains a
phosphopantetheine moiety (as does CoA) as the reactive unit, attached
to the ACP protein through a serine. The holo-ACP synthase enzyme
(encoded by the acpS gene) transfers the 4-phosphopantetheine
moeity of CoA to the apo-ACP to form holo-ACP, which is the active
form of the carrier in lipid synthesis |CITS: [68313114] [81215492]|.)""",
('B1094', 'AACPS2') : """(Lipoate synthase catalyzes the step of lipoic acid biosynthesis at which sulfur is inserted into octanoyl-ACP to form the lipoate moiety |CITS: [8444795], [11106496]|. Lipoate modification (by lipoyl-protein ligases LipB or LplA) of complex subunits is important for function of pyruvate dehydrogenase |CITS: [814874], [6794598], [8444795]|, alpha-ketoglutarate dehydrogenase |CITS: [814874], [6794598], [8444795]|, and the glycine cleavage system |CITS: [1655709], [8444795]|.)""",
('B1094', 'AACPS2') : """(Lipoate synthase catalyzes the step of lipoic acid biosynthesis at which sulfur is inserted into octanoyl-ACP to form the lipoate moiety |CITS: [8444795], [11106496]|. Lipoate synthase is a LipA homodimer with two (4Fe-4S) iron-sulfur clusters per protein dimer under anaerobic conditions, and these clusters are oxidized to the (2Fe-2S) state in air |CITS: [10747808], [10403368]|. The enzyme uses octanoyl-ACP, but not octanoic acid, as substrate and also uses S-adenosyl methionine |CITS: [11106496]|.)""",
('B1094', 'AACPS2') : """NIL""",
('B1094', 'AACPS2') : """NIL""",
('B1094', 'AACPS2') : """NIL""",
('B1094', 'AACPS2') : """NIL""",
('B1094', 'AACPS2') : """NIL""",
('B1094', 'AACPS2') : """NIL""",
('B1094', 'AACPS2') : """NIL""",
('B1094', 'AACPS2') : """NIL""",
('B1094', 'AACPS2') : """NIL""",
('B1094', 'AACPS2') : """NIL""",
('B1094', 'AACPS2') : """NIL""",
('B1094', 'AACPS2') : """NIL""",
('B1094', 'AACPS2') : """NIL""",
('B1094', 'AACPS2') : """NIL""",
('B1094', 'AACPS2') : """NIL""",
('B1094', 'AACPS2') : """NIL""",
('B1094', 'AACPS2') : """(The holo-ACP synthase enzyme (encoded by acpS) transfers the 4-phosphopantetheine
moiety of CoA to the apo-ACP to form holo-ACP, which is the active
form of the carrier in lipid synthesis |CITS: [68313114] [81215492]|.)""",
('B1094', 'AACPS3') : """(Acyl carrier protein (ACP) plays an important role in fatty
acid biosynthesis. It carries fatty acid chains via a thioester
linkage to a phosphopantetheine prosthetic group as the chains are
elongated. There is also evidence that it has a function in the
biosynthesis of membrane-derived oligosaccharides. Therefore ACP and
its acyl forms interact with at least 12 different E. coli enzymes.
|CITS: [92210530] [89050961] [88296479]| ACP is the most abundant
protein in E. coli, with about 1.5E6 molecules per cell. |CITS: [Mathews&vanHolde]| ACP contains a
phosphopantetheine moiety (as does CoA) as the reactive unit, attached
to the ACP protein through a serine. The holo-ACP synthase enzyme
(encoded by the acpS gene) transfers the 4-phosphopantetheine
moeity of CoA to the apo-ACP to form holo-ACP, which is the active
form of the carrier in lipid synthesis |CITS: [68313114] [81215492]|.)""",
('B1094', 'AACPS3') : """(Lipoate synthase catalyzes the step of lipoic acid biosynthesis at which sulfur is inserted into octanoyl-ACP to form the lipoate moiety |CITS: [8444795], [11106496]|. Lipoate modification (by lipoyl-protein ligases LipB or LplA) of complex subunits is important for function of pyruvate dehydrogenase |CITS: [814874], [6794598], [8444795]|, alpha-ketoglutarate dehydrogenase |CITS: [814874], [6794598], [8444795]|, and the glycine cleavage system |CITS: [1655709], [8444795]|.)""",
('B1094', 'AACPS3') : """(Lipoate synthase catalyzes the step of lipoic acid biosynthesis at which sulfur is inserted into octanoyl-ACP to form the lipoate moiety |CITS: [8444795], [11106496]|. Lipoate synthase is a LipA homodimer with two (4Fe-4S) iron-sulfur clusters per protein dimer under anaerobic conditions, and these clusters are oxidized to the (2Fe-2S) state in air |CITS: [10747808], [10403368]|. The enzyme uses octanoyl-ACP, but not octanoic acid, as substrate and also uses S-adenosyl methionine |CITS: [11106496]|.)""",
('B1094', 'AACPS3') : """NIL""",
('B1094', 'AACPS3') : """NIL""",
('B1094', 'AACPS3') : """NIL""",
('B1094', 'AACPS3') : """NIL""",
('B1094', 'AACPS3') : """NIL""",
('B1094', 'AACPS3') : """NIL""",
('B1094', 'AACPS3') : """NIL""",
('B1094', 'AACPS3') : """NIL""",
('B1094', 'AACPS3') : """NIL""",
('B1094', 'AACPS3') : """NIL""",
('B1094', 'AACPS3') : """NIL""",
('B1094', 'AACPS3') : """NIL""",
('B1094', 'AACPS3') : """NIL""",
('B1094', 'AACPS3') : """NIL""",
('B1094', 'AACPS3') : """NIL""",
('B1094', 'AACPS3') : """NIL""",
('B1094', 'AACPS3') : """(The holo-ACP synthase enzyme (encoded by acpS) transfers the 4-phosphopantetheine
moiety of CoA to the apo-ACP to form holo-ACP, which is the active
form of the carrier in lipid synthesis |CITS: [68313114] [81215492]|.)""",
('B4358', 'GALCTLO') : """(YjjN did not show dehydrogenase activity in a high-throughput screen of purified proteins |CITS: [15808744]|.
)""",
('B0335', 'ACCOAL') : """(Acs appears to be more likely than PrpE to catalyze the first step in the propionate metabolism pathway |CITS: [12473114]|.
Regulation has been described |CITS: [12473114]|. Gene expression is induced by propionate, but protein is not observed during growth on propionate or acetate |CITS: [12473114]|.
)""",
('B2492', 'FORtppi') : """(FocB is a putative formate transporter, belonging to the FNT
family of formate and nitrite transporters |CITS: [99184734]|.
The focB gene is located in the putative twelve gene hyf
operon, which includes nine genes encoding a putative formate
hydrogenlyase complex |CITS: [98048487]|. FocB is highly similar
to the formate transporter FocA, and presumably functions as a
formate transporter reponsible for uptake of formate to provide
a substrate for the formate hydrogenlyase.)""",
('B0732', 'MANPGH') : """(The mngB gene encodes an alpha-mannosidase |CITS: [14645248]|.)""",
('B2034', 'O16GALFT') : """(WbbI (GalF) is not required for colanic acid biosynthesis |CITS: [8759852]|.
In E. coli O7:K1, GalF binds to and regulates GalU UDP-glucose pyrophosphorylase |CITS: [8971705]|. In E. coli K30, GalF is involved in biosynthesis of capsular polysaccharide, and transcription of the galF gene is activated by RcsB |CITS: [12581358]|.)""",
('B0839', 'MDDCP1pp') : """(DacC is a penicillin-binding protein that is required for proper cell morphology and provides
some resistance to penicillin |CITS: [1447130][12354237][6215397]|. It is one of four DD-carboxypeptidase
low-molecular weight PBPs in Escherichia coli (along with PBP4, PBP6 and DacD) that modify
peptidoglycans through the removal of the terminal D-alanine from pentapeptide side chains |CITS:[368033]|,
|CITS:[8955390]|.
The carboxy-terminus of DacC is capable of forming an alpha helix and interacts with
membranes chiefly through hydrophobic forces |CITS: [9371419][9858668]|.
Deletion of this membrane-anchoring portion of the protein produces soluble DacC. Whereas
overexpression of native DacC results in membrane vesicles in the cystoplasm, overexpression
of this soluble variant yields inclusion bodies. Both forms of DacC can be purified with
Procion rubine MX-B and subsequently bind stoichiometrically with penicillin |CITS: [1447130]|.
Despite being part of a family of D-alanine carboxypeptidases, DacC lacks detectable activity
against bisacetyl-L-lysine-D-alanyl-D-alanine and other test substrates |CITS: [1447130]|.
Deletions in dacC are viable, though slightly penicillin sensitive |CITS: [6215397]|.
dacC dacA double mutants are viable, though they show defects in morphology and cell division
when bolA, which is required for dacC expression on entry to stationary phase, is overexpressed |CITS: [3903044][12354237][2684651]|.
A complete deletion of dacA-D is also viable, as is a strain lacking eight of the known penicillin-binding protein genes,
dacC among them |CITS: [8955390][10383966]|. Overexpression of DacC allows cell division in ftsI23 mutants, but leads to cell
lysis during early exponential growth |CITS: [2254246][11325933]|.)""",
('B2835', '2AGPG161tipp') : """(LplT is a major facilitator superfamily (MFS) protein that acts as a flippase for transbilayer movement of
lysophospholipids. Mutation experiments and
transporter assays have determined LplT is responsible for the facilitated diffusion of lysophospholipids to
the cytoplasmic portion of the inner membrane providing substrate for the bifunctional enzyme
2-acyl-GPE acyltransferase/acyl-ACP synthetase (Aas). lplT forms an operon with the aas
gene |CITS:[15661733]|.)""",
('B0684', 'RNTR3c') : """(Flavodoxins are small, acidic electron transfer proteins which contain FMN as a prosthetic group. They are only
able to accept and donate electrons. Flavodoxin is an important member of the multi-enzyme complexes that are
involved in the activation of anaerobic nucleoside reductase and pyruvate-formate lyase. Flavodoxins are
functionally interchangeable with ferredoxins, but some enzymes are specific for one or the other. E. coli has
at least two flavodoxins |CITS: [91154129][95050480][93194782]|.
FldA is essential under both aerobic and anaerobic growth conditions |CITS: [10714981]|. The essential role for
flavodoxin 1 under aerobic conditions is in the MEP pathway for isoprenoid biosynthesis
(|FRAME: NONMEVIPP-PWY|) |CITS: [15978585]|.
Crystal and solution structures of FldA have been solved |CITS: [9416602][9119004]|.)""",
('B0684', 'RNTR3c') : """NIL""",
('B2895', 'RNTR3c') : """(Flavodoxins are small, acidic electron transfer proteins
which contain FMN as a prosthetic group. They are only able to accept
and donate electrons. Flavodoxin is an important member of the
multi-enzyme complexes that are involved in the activation of
anaerobic nucleoside reductase and pyruvate-formate lyase. Flavodoxins
are functionally interchangeable with ferredoxins but some enzymes are
specific for one or the other. E. coli has at least two flavodoxins.
|CITS: [91154129] [95050480] [93194782]|)""",
('B2895', 'RNTR3c') : """NIL""",
('B2895', 'RNTR3c') : """(Flavodoxins are small, acidic electron transfer proteins
which contain FMN as a prosthetic group. They are only able to accept
and donate electrons. Flavodoxin is an important member of the
multi-enzyme complexes that are involved in the activation of
anaerobic nucleoside reductase and pyruvate-formate lyase. Flavodoxins
are functionally interchangeable with ferredoxins but some enzymes are
specific for one or the other. E. coli has at least two flavodoxins.
|CITS: [91154129] [95050480] [93194782]|)""",
('B2895', 'RNTR3c') : """NIL""",
('B0684', 'RNTR3c') : """(Flavodoxins are small, acidic electron transfer proteins which contain FMN as a prosthetic group. They are only
able to accept and donate electrons. Flavodoxin is an important member of the multi-enzyme complexes that are
involved in the activation of anaerobic nucleoside reductase and pyruvate-formate lyase. Flavodoxins are
functionally interchangeable with ferredoxins, but some enzymes are specific for one or the other. E. coli has
at least two flavodoxins |CITS: [91154129][95050480][93194782]|.
FldA is essential under both aerobic and anaerobic growth conditions |CITS: [10714981]|. The essential role for
flavodoxin 1 under aerobic conditions is in the MEP pathway for isoprenoid biosynthesis
(|FRAME: NONMEVIPP-PWY|) |CITS: [15978585]|.
Crystal and solution structures of FldA have been solved |CITS: [9416602][9119004]|.)""",
('B0684', 'RNTR3c') : """NIL""",
('B2835', '2AGPE140tipp') : """(LplT is a major facilitator superfamily (MFS) protein that acts as a flippase for transbilayer movement of
lysophospholipids. Mutation experiments and
transporter assays have determined LplT is responsible for the facilitated diffusion of lysophospholipids to
the cytoplasmic portion of the inner membrane providing substrate for the bifunctional enzyme
2-acyl-GPE acyltransferase/acyl-ACP synthetase (Aas). lplT forms an operon with the aas
gene |CITS:[15661733]|.)""",
('B2835', '2AGPA140tipp') : """(LplT is a major facilitator superfamily (MFS) protein that acts as a flippase for transbilayer movement of
lysophospholipids. Mutation experiments and
transporter assays have determined LplT is responsible for the facilitated diffusion of lysophospholipids to
the cytoplasmic portion of the inner membrane providing substrate for the bifunctional enzyme
2-acyl-GPE acyltransferase/acyl-ACP synthetase (Aas). lplT forms an operon with the aas
gene |CITS:[15661733]|.)""",
('B2128', 'GLYBabcpp') : """(membrane component of ABC transporter)""",
('B2128', 'GLYBabcpp') : """(YehX, YehW, YehY, YehZ are uncharacterized members
of the ABC superfamily of transporters |CITS: [99091701]|.
YehX is the putative ATP binding component, YehW and YehY
are the membrane components, and YehZ is the putative
periplasmic binding protein. Based on sequence similarity
they probably function together as an ATP-dependant
osmoprotection transporter. The yehX, yehW,
yehY, and yehZ genes are located
within a single operon.
Osmotic shock and entry into stationary phase induced transcription of the yehZYXW operon,
which was dependent upon σs |CITS:[15251200]|.)""",
('B2129', 'GLYBabcpp') : """(ATP-binding component of ABC transporter)""",
('B2129', 'GLYBabcpp') : """(YehX, YehW, YehY, YehZ are uncharacterized members
of the ABC superfamily of transporters |CITS: [99091701]|.
YehX is the putative ATP binding component, YehW and YehY
are the membrane components, and YehZ is the putative
periplasmic binding protein. Based on sequence similarity
they probably function together as an ATP-dependant
osmoprotection transporter. The yehX, yehW,
yehY, and yehZ genes are located
within a single operon.
Osmotic shock and entry into stationary phase induced transcription of the yehZYXW operon,
which was dependent upon σs |CITS:[15251200]|.)""",
('B2130', 'GLYBabcpp') : """(membrane component of ABC transporter)""",
('B2130', 'GLYBabcpp') : """(YehX, YehW, YehY, YehZ are uncharacterized members
of the ABC superfamily of transporters |CITS: [99091701]|.
YehX is the putative ATP binding component, YehW and YehY
are the membrane components, and YehZ is the putative
periplasmic binding protein. Based on sequence similarity
they probably function together as an ATP-dependant
osmoprotection transporter. The yehX, yehW,
yehY, and yehZ genes are located
within a single operon.
Osmotic shock and entry into stationary phase induced transcription of the yehZYXW operon,
which was dependent upon σs |CITS:[15251200]|.)""",
('B2131', 'GLYBabcpp') : """(periplasmic binding component of ABC transporter)""",
('B2131', 'GLYBabcpp') : """(YehX, YehW, YehY, YehZ are uncharacterized members
of the ABC superfamily of transporters |CITS: [99091701]|.
YehX is the putative ATP binding component, YehW and YehY
are the membrane components, and YehZ is the putative
periplasmic binding protein. Based on sequence similarity
they probably function together as an ATP-dependant
osmoprotection transporter. The yehX, yehW,
yehY, and yehZ genes are located
within a single operon.
Osmotic shock and entry into stationary phase induced transcription of the yehZYXW operon,
which was dependent upon σs |CITS:[15251200]|.)""",
('B2788', 'GLCRD') : """(No information about this protein was found by a literature search conducted on January 9, 2006.)""",
('B4192', 'ASCBPL') : """(UlaG is required for the ability to utilize L-ascorbate as the sole carbon source under anaerobic growth conditions
|CITS: [12644495]|. The enzyme was suggested to be a cytoplasmic L-ascorbate 6-phosphate lactonase
|CITS: [12644495]|. Phosphodiesterase activity of UlaG was discovered in a high-throughput screen of purified
proteins |CITS: [15808744]|.
Expression of ulaG is negatively regulated by UlaR |CITS: [12374842]|.)""",
('B3781', 'RNDR4') : """(Thioredoxin is a small electron-transfer protein which contains a cysteine
disulfide/dithiol active site. The protein functions in a wide variety of cellular
processes. Thioredoxin is reduced by NADPH in a reaction catalyzed by
thioredoxin reductase. The conversion between the oxidized and reduced
forms results in a change of conformation. The functional properties differ
between the two forms of thioredoxin. The reduced thioredoxin is a powerful
protein disulfide reductase, thioredoxin catalyzes dithiol-disulfide exchange
reactions. The oxidized form of thioredoxin has been crystallized,
the reduced form has been solved by NMR. |CITS: [85277988] [90198521]
[90254096] [90298180] [93264420] [90204538]|)""",
('B3781', 'RNDR4') : """(Thioredoxin is a small electron-transfer protein which contains a cysteine
disulfide/dithiol active site. The protein functions in a wide variety of cellular
processes. Thioredoxin is reduced by NADPH in a reaction catalyzed by
thioredoxin reductase. The conversion between the oxidized and reduced
forms results in a change of conformation. The functional properties differ
between the two forms of thioredoxin. The reduced thioredoxin is a powerful
protein disulfide reductase, thioredoxin catalyzes dithiol-disulfide exchange
reactions. The oxidized form of thioredoxin has been crystallized, the reduced
form has been solved by NMR.
|CITS: [85277988] [90198521] [90254096] [90298180] [93264420] [90204538]|)""",
('B2582', 'RNDR4') : """(The trxC gene encodes a second thioredoxin in E. coli. Thioredoxin 2 can perform many of
thioredoxin 1's roles in vivo; it is able to reduce some essential cytoplasmic enzymes.
Along with thioredoxin 1 and glutaredoxin 1, thioredoxin 2 is one of E. coli's most
effective cytoplasmic disulfide-reducing proteins. Any one of these three is sufficient
to support aerobic growth. |CITS: [98429478] [98049550]|)""",
('B2582', 'RNDR4') : """NIL""",
('B3781', 'RNDR3') : """(Thioredoxin is a small electron-transfer protein which contains a cysteine
disulfide/dithiol active site. The protein functions in a wide variety of cellular
processes. Thioredoxin is reduced by NADPH in a reaction catalyzed by
thioredoxin reductase. The conversion between the oxidized and reduced
forms results in a change of conformation. The functional properties differ
between the two forms of thioredoxin. The reduced thioredoxin is a powerful
protein disulfide reductase, thioredoxin catalyzes dithiol-disulfide exchange
reactions. The oxidized form of thioredoxin has been crystallized,
the reduced form has been solved by NMR. |CITS: [85277988] [90198521]
[90254096] [90298180] [93264420] [90204538]|)""",
('B3781', 'RNDR3') : """(Thioredoxin is a small electron-transfer protein which contains a cysteine
disulfide/dithiol active site. The protein functions in a wide variety of cellular
processes. Thioredoxin is reduced by NADPH in a reaction catalyzed by
thioredoxin reductase. The conversion between the oxidized and reduced
forms results in a change of conformation. The functional properties differ
between the two forms of thioredoxin. The reduced thioredoxin is a powerful
protein disulfide reductase, thioredoxin catalyzes dithiol-disulfide exchange
reactions. The oxidized form of thioredoxin has been crystallized, the reduced
form has been solved by NMR.
|CITS: [85277988] [90198521] [90254096] [90298180] [93264420] [90204538]|)""",
('B2582', 'RNDR3') : """(The trxC gene encodes a second thioredoxin in E. coli. Thioredoxin 2 can perform many of
thioredoxin 1's roles in vivo; it is able to reduce some essential cytoplasmic enzymes.
Along with thioredoxin 1 and glutaredoxin 1, thioredoxin 2 is one of E. coli's most
effective cytoplasmic disulfide-reducing proteins. Any one of these three is sufficient
to support aerobic growth. |CITS: [98429478] [98049550]|)""",
('B2582', 'RNDR3') : """NIL""",
('B3781', 'RNDR2') : """(Thioredoxin is a small electron-transfer protein which contains a cysteine
disulfide/dithiol active site. The protein functions in a wide variety of cellular
processes. Thioredoxin is reduced by NADPH in a reaction catalyzed by
thioredoxin reductase. The conversion between the oxidized and reduced
forms results in a change of conformation. The functional properties differ
between the two forms of thioredoxin. The reduced thioredoxin is a powerful
protein disulfide reductase, thioredoxin catalyzes dithiol-disulfide exchange
reactions. The oxidized form of thioredoxin has been crystallized,
the reduced form has been solved by NMR. |CITS: [85277988] [90198521]
[90254096] [90298180] [93264420] [90204538]|)""",
('B3781', 'RNDR2') : """(Thioredoxin is a small electron-transfer protein which contains a cysteine
disulfide/dithiol active site. The protein functions in a wide variety of cellular
processes. Thioredoxin is reduced by NADPH in a reaction catalyzed by
thioredoxin reductase. The conversion between the oxidized and reduced
forms results in a change of conformation. The functional properties differ
between the two forms of thioredoxin. The reduced thioredoxin is a powerful
protein disulfide reductase, thioredoxin catalyzes dithiol-disulfide exchange
reactions. The oxidized form of thioredoxin has been crystallized, the reduced
form has been solved by NMR.
|CITS: [85277988] [90198521] [90254096] [90298180] [93264420] [90204538]|)""",
('B2582', 'RNDR2') : """(The trxC gene encodes a second thioredoxin in E. coli. Thioredoxin 2 can perform many of
thioredoxin 1's roles in vivo; it is able to reduce some essential cytoplasmic enzymes.
Along with thioredoxin 1 and glutaredoxin 1, thioredoxin 2 is one of E. coli's most
effective cytoplasmic disulfide-reducing proteins. Any one of these three is sufficient
to support aerobic growth. |CITS: [98429478] [98049550]|)""",
('B2582', 'RNDR2') : """NIL""",
('B2582', 'RNDR1') : """(The trxC gene encodes a second thioredoxin in E. coli. Thioredoxin 2 can perform many of
thioredoxin 1's roles in vivo; it is able to reduce some essential cytoplasmic enzymes.
Along with thioredoxin 1 and glutaredoxin 1, thioredoxin 2 is one of E. coli's most
effective cytoplasmic disulfide-reducing proteins. Any one of these three is sufficient
to support aerobic growth. |CITS: [98429478] [98049550]|)""",
('B2582', 'RNDR1') : """NIL""",
('B3781', 'RNDR1') : """(Thioredoxin is a small electron-transfer protein which contains a cysteine
disulfide/dithiol active site. The protein functions in a wide variety of cellular
processes. Thioredoxin is reduced by NADPH in a reaction catalyzed by
thioredoxin reductase. The conversion between the oxidized and reduced
forms results in a change of conformation. The functional properties differ
between the two forms of thioredoxin. The reduced thioredoxin is a powerful
protein disulfide reductase, thioredoxin catalyzes dithiol-disulfide exchange
reactions. The oxidized form of thioredoxin has been crystallized,
the reduced form has been solved by NMR. |CITS: [85277988] [90198521]
[90254096] [90298180] [93264420] [90204538]|)""",
('B3781', 'RNDR1') : """(Thioredoxin is a small electron-transfer protein which contains a cysteine
disulfide/dithiol active site. The protein functions in a wide variety of cellular
processes. Thioredoxin is reduced by NADPH in a reaction catalyzed by
thioredoxin reductase. The conversion between the oxidized and reduced
forms results in a change of conformation. The functional properties differ
between the two forms of thioredoxin. The reduced thioredoxin is a powerful
protein disulfide reductase, thioredoxin catalyzes dithiol-disulfide exchange
reactions. The oxidized form of thioredoxin has been crystallized, the reduced
form has been solved by NMR.
|CITS: [85277988] [90198521] [90254096] [90298180] [93264420] [90204538]|)""",
('B1064', 'RNDR1b') : """(Glutaredoxins are ubiquitous proteins that catalyze the reduction of disulfides via reduced glutathione (GSH).
Escherichia coli has three glutaredoxins (Grx1, Grx2, and Grx3) containing the classic dithiol active site
CPYC, and a fourth one which contains a monothiol (CGFS) potential active site |CITS: [15833738]|.
The glutaredoxins do not act as enzymes, but rather as a cofactor, enabling intracellular redox reactions through
a disulfide/dithiol enzymatic mechanism involving the active site cysteines.
There is almost no similarity between the amino acid sequence of Grx2 (an approximately 27 kDa protein) and Grx1
or Grx3 (both 9-kDa proteins), with the exception of the active site which is identical in all three glutaredoxins.
In contrast to glutaredoxin 1 and 3, Grx 2 is not a hydrogen donor for ribonucleotide reductase.
On the other hand, Grx2 is the primary hydrogen donor to ArsC-catalyzed arsenate reduction (|FRAME: RXN-982|)
|CITS: [10593884]|. It is also the most abundant glutaredoxin in the cell, with an intracellular concentration
of 5 µM, compared with 0.2 µM and 2.4 µM for Grx1 and 3, respectively |CITS: [10593884]|.)""",
('B1064', 'RNDR1b') : """(Glutaredoxins are ubiquitous proteins that catalyze the reduction of disulfides via reduced glutathione (GSH).
Escherichia coli has three glutaredoxins (Grx1, Grx2, and Grx3) containing the classic dithiol active site
CPYC, and a fourth one which contains a monothiol (CGFS) potential active site |CITS: [15833738]|.
The glutaredoxins do not act as enzymes, but rather as a cofactor, enabling intracellular redox reactions through
a disulfide/dithiol enzymatic mechanism involving the active site cysteines.
There is almost no similarity between the amino acid sequence of Grx2 (an approximately 27 kDa protein) and Grx1
or Grx3 (both 9-kDa proteins), with the exception of the active site which is identical in all three glutaredoxins.
In contrast to glutaredoxin 1 and 3, Grx 2 is not a hydrogen donor for ribonucleotide reductase.
On the other hand, Grx2 is the primary hydrogen donor to ArsC-catalyzed arsenate reduction (|FRAME: RXN-982|)
|CITS: [10593884]|. It is also the most abundant glutaredoxin in the cell, with an intracellular concentration
of 5 µM, compared with 0.2 µM and 2.4 µM for Grx1 and 3, respectively |CITS: [10593884]|.)""",
('B3610', 'RNDR1b') : """(There at least three glutaredoxins in E. coli. Glutaredoxin
3 is able to function as a disulfide reductase, but not as well as
glutaredoxin 1. Coupled with cellular glutathione it may be the third
hydrogen donor system in the absence of thioredoxin and glutaredoxin
1. Under normal conditions it is likely that glutaredoxin has other
functions. |CITS: [95024051] [96215095]|)""",
('B3610', 'RNDR1b') : """NIL""",
('B1654', 'RNDR1b') : """(Grx4 belongs to the family of monothiol glutaredoxins. Oxidized Grx4 can be reduced by the thioredoxin system or
glutaredoxin 1. Grx4 is not active in the standard glutaredoxin assay |CITS: [15833738]|.
Grx4 is an abundant protein that is upregulated during stationary phase; the increased expression is dependent on
ppGpp |CITS: [15833738]|.
A grxD null mutant could not be obtained |CITS: [15833738]|. grxD has previously been reported to be
essential for aerobic growth in rich media |CITS: [13129938]|.
A solution structure of the reduced form of Grx4 has been determined |CITS: [15840565]|)""",
('B0849', 'RNDR1b') : """NIL""",
('B0849', 'RNDR1b') : """(Glutaredoxins are ubiquitous proteins that catalyze the reduction of disulfides via reduced glutathione (GSH).
Escherichia coli has three glutaredoxins (Grx1, Grx2, and Grx3) containing the classic dithiol active site
CPYC, and a fourth one which contains a monothiol (CGFS) potential active site |CITS: [15833738]|.
The glutaredoxins act as a cofactor enabling intracellular redox reactions through a disulfide/dithiol
enzymatic mechanism involving the active site cysteines. They are used as a
hydrogen donor for the glutathione(GSH)-dependent synthesis of deoxyribonucleotides
by ribonucleotide reductase and reduces specific cysteine residues in
ribonucleotide reductase.
Glutaredoxin are also a hydrogen donor for the reduction of adenosine 3'-phosphate 5'-phosphosulfate
and methionine sulfoxide.
In addition, glutaredoxins also catalyzes GSH-disulfide oxidoreduction reactions with low molecular weight
substrates. |CITS: [79151138] [91242463] [93003075]| There are two additional
glutaredoxins in E. coli whose physiological roles have not been fully
determined. |CITS: [95024051]|)""",
('B4356', 'GALCTNLt2pp') : """(The YjiZ protein is an uncharacterised member of the
major facilitator superfamily (MFS) of transporters |CITS: [98190790]|.
Based on sequence similarity, YjiZ may function as a proton-driven
metabolite uptake system.)""",
('B2835', '2AGPA160tipp') : """(LplT is a major facilitator superfamily (MFS) protein that acts as a flippase for transbilayer movement of
lysophospholipids. Mutation experiments and
transporter assays have determined LplT is responsible for the facilitated diffusion of lysophospholipids to
the cytoplasmic portion of the inner membrane providing substrate for the bifunctional enzyme
2-acyl-GPE acyltransferase/acyl-ACP synthetase (Aas). lplT forms an operon with the aas
gene |CITS:[15661733]|.)""",
('B2128', 'CHLabcpp') : """(membrane component of ABC transporter)""",
('B2128', 'CHLabcpp') : """(YehX, YehW, YehY, YehZ are uncharacterized members
of the ABC superfamily of transporters |CITS: [99091701]|.
YehX is the putative ATP binding component, YehW and YehY
are the membrane components, and YehZ is the putative
periplasmic binding protein. Based on sequence similarity
they probably function together as an ATP-dependant
osmoprotection transporter. The yehX, yehW,
yehY, and yehZ genes are located
within a single operon.
Osmotic shock and entry into stationary phase induced transcription of the yehZYXW operon,
which was dependent upon σs |CITS:[15251200]|.)""",
('B2129', 'CHLabcpp') : """(ATP-binding component of ABC transporter)""",
('B2129', 'CHLabcpp') : """(YehX, YehW, YehY, YehZ are uncharacterized members
of the ABC superfamily of transporters |CITS: [99091701]|.
YehX is the putative ATP binding component, YehW and YehY
are the membrane components, and YehZ is the putative
periplasmic binding protein. Based on sequence similarity
they probably function together as an ATP-dependant
osmoprotection transporter. The yehX, yehW,
yehY, and yehZ genes are located
within a single operon.
Osmotic shock and entry into stationary phase induced transcription of the yehZYXW operon,
which was dependent upon σs |CITS:[15251200]|.)""",
('B2130', 'CHLabcpp') : """(membrane component of ABC transporter)""",
('B2130', 'CHLabcpp') : """(YehX, YehW, YehY, YehZ are uncharacterized members
of the ABC superfamily of transporters |CITS: [99091701]|.
YehX is the putative ATP binding component, YehW and YehY
are the membrane components, and YehZ is the putative
periplasmic binding protein. Based on sequence similarity
they probably function together as an ATP-dependant
osmoprotection transporter. The yehX, yehW,
yehY, and yehZ genes are located
within a single operon.
Osmotic shock and entry into stationary phase induced transcription of the yehZYXW operon,
which was dependent upon σs |CITS:[15251200]|.)""",
('B2131', 'CHLabcpp') : """(periplasmic binding component of ABC transporter)""",
('B2131', 'CHLabcpp') : """(YehX, YehW, YehY, YehZ are uncharacterized members
of the ABC superfamily of transporters |CITS: [99091701]|.
YehX is the putative ATP binding component, YehW and YehY
are the membrane components, and YehZ is the putative
periplasmic binding protein. Based on sequence similarity
they probably function together as an ATP-dependant
osmoprotection transporter. The yehX, yehW,
yehY, and yehZ genes are located
within a single operon.
Osmotic shock and entry into stationary phase induced transcription of the yehZYXW operon,
which was dependent upon σs |CITS:[15251200]|.)""",
('B0936', 'BUTSO3abcpp') : """NIL""",
('B0936', 'BUTSO3abcpp') : """(Deletion mutation studies |CITS:[10506196]| indicate that the ssuEADCB gene cluster codes for proteins that enable Escherichia coli
to utilize sulfonates other than taurine as a sulfur source. Based on sequence similarity SsuABC is the ABC type transport system with
SsuA being the periplasmic substrate-binding subunit, SsuB the ATP-binding subunit and SsuC the permease. ssuD and
ssuE encode an FMNH2-dependent monooxygenase and an NAD(P)H-dependent FMN reductase, respectively.)""",
('B0933', 'BUTSO3abcpp') : """(ATP-binding component of ABC transporter)""",
('B0933', 'BUTSO3abcpp') : """(Deletion mutation studies |CITS:[10506196]| indicate that the ssuEADCB gene cluster codes for proteins that enable Escherichia coli
to utilize sulfonates other than taurine as a sulfur source. Based on sequence similarity SsuABC is the ABC type transport system with
SsuA being the periplasmic substrate-binding subunit, SsuB the ATP-binding subunit and SsuC the permease. ssuD and
ssuE encode an FMNH2-dependent monooxygenase and an NAD(P)H-dependent FMN reductase, respectively.)""",
('B0934', 'BUTSO3abcpp') : """(membrane component of ABC transporter
Protein topology in the inner membrane has been determined |CITS: [11867724]|.)""",
('B0934', 'BUTSO3abcpp') : """(Deletion mutation studies |CITS:[10506196]| indicate that the ssuEADCB gene cluster codes for proteins that enable Escherichia coli
to utilize sulfonates other than taurine as a sulfur source. Based on sequence similarity SsuABC is the ABC type transport system with
SsuA being the periplasmic substrate-binding subunit, SsuB the ATP-binding subunit and SsuC the permease. ssuD and
ssuE encode an FMNH2-dependent monooxygenase and an NAD(P)H-dependent FMN reductase, respectively.)""",
('B3396', 'MCTP1Bpp') : """(PBP1A is the product of the mrcA gene |CITS:[3882429]|. PBP1A is a bifunctional, inner membrane enzyme
catalyzing the transglycosylation and transpeptidation of murein (peptidoglycan) precursors in the formation of the
murein sacculus |CITS:[9529891]|. The amino terminus contains a signal sequence |CITS:[3882429]|. PBP1A is able
to dimerize without disulfide bonds, but doesn't form a complex with PBP1B |CITS:[12057973]|. Either PBP1A or
PBP1B (the other major bifunctional enzyme in murein synthesis with a different penicillin-binding affinity) is required
for cell elongation because a PBP1A-PBP1B double mutation is lethal |CITS:[1103132][341159][345275][2993822]|.
Experiments have been performed involving inhibition or mutation of PBP1A alone or coupled with inhibition or
mutation of other proteins involved in cell division and murein metabolism |CITS:[7007327][2211517][2066344][10383966]|.)""",
('B0684', 'FLDR') : """(Flavodoxins are small, acidic electron transfer proteins which contain FMN as a prosthetic group. They are only
able to accept and donate electrons. Flavodoxin is an important member of the multi-enzyme complexes that are
involved in the activation of anaerobic nucleoside reductase and pyruvate-formate lyase. Flavodoxins are
functionally interchangeable with ferredoxins, but some enzymes are specific for one or the other. E. coli has
at least two flavodoxins |CITS: [91154129][95050480][93194782]|.
FldA is essential under both aerobic and anaerobic growth conditions |CITS: [10714981]|. The essential role for
flavodoxin 1 under aerobic conditions is in the MEP pathway for isoprenoid biosynthesis
(|FRAME: NONMEVIPP-PWY|) |CITS: [15978585]|.
Crystal and solution structures of FldA have been solved |CITS: [9416602][9119004]|.)""",
('B0684', 'FLDR') : """NIL""",
('B2895', 'FLDR') : """(Flavodoxins are small, acidic electron transfer proteins
which contain FMN as a prosthetic group. They are only able to accept
and donate electrons. Flavodoxin is an important member of the
multi-enzyme complexes that are involved in the activation of
anaerobic nucleoside reductase and pyruvate-formate lyase. Flavodoxins
are functionally interchangeable with ferredoxins but some enzymes are
specific for one or the other. E. coli has at least two flavodoxins.
|CITS: [91154129] [95050480] [93194782]|)""",
('B2895', 'FLDR') : """NIL""",
('B1773', 'FBA') : """(No information about this protein was found by a literature search conducted on December 28, 2005.
)""",
('B2835', '2AGPE141tipp') : """(LplT is a major facilitator superfamily (MFS) protein that acts as a flippase for transbilayer movement of
lysophospholipids. Mutation experiments and
transporter assays have determined LplT is responsible for the facilitated diffusion of lysophospholipids to
the cytoplasmic portion of the inner membrane providing substrate for the bifunctional enzyme
2-acyl-GPE acyltransferase/acyl-ACP synthetase (Aas). lplT forms an operon with the aas
gene |CITS:[15661733]|.)""",
('B2579', 'PFL') : """(The yfiD gene encodes a glycyl radical protein that can replace an oxidatively damaged pyruvate formate-lyase subunit |CITS: [11444864]|. YfiD is expected to be involved in stress resistance |CITS: [10726772]|.
Residue Gly102 is predicted to be the glycyl radical site |CITS: [11444864]|. Pyruvate formate-lyase-activase catalyzes YfiD glycyl radical formation |CITS: [11932447]|. Formation of the YfiD glycyl radical is induced by acidic pH (as is yfiD expression) |CITS: [11932447]|. Pyruvate formate-lyase-deactivase does not appear to catalyze YfiD glycyl radical inactivation |CITS: [11932447]|. YfiD is phosphorylated in L-form (wall-less) E. coli |CITS: [9884220]|.
A yfiD mutant shows a defect in acid homeostasis under low-oxygen conditions |CITS: [11932447]|.
YfiD has similarity to pyruvate formate lyase |CITS: [10094700]|.
Regulation has been described |CITS: [9179852], [9767578], [10094700], [10726772], [11114930], [11169114], [11591692], [12107143], [12949096]|.)""",
('B3951', 'PFL') : """(PflD was identified by sequence similarity as a homolog of pyruvate formate-lyase |CITS: [7773398]|. Effects of a gene
knockout have been studied; the fermentation pattern under microaerobic conditions is similar to wild type
|CITS: [14673546]|.)""",
('B3952', 'PFL') : """(PflC was identified by sequence similarity as a homolog of pyruvate formate-lyase activating enzyme
|CITS: [7773398]|. Effects of a gene knockout have been studied; the fermentation pattern under microaerobic
conditions is similar to wild type |CITS: [14673546]|.)""",
('B1064', 'GRXR') : """(Glutaredoxins are ubiquitous proteins that catalyze the reduction of disulfides via reduced glutathione (GSH).
Escherichia coli has three glutaredoxins (Grx1, Grx2, and Grx3) containing the classic dithiol active site
CPYC, and a fourth one which contains a monothiol (CGFS) potential active site |CITS: [15833738]|.
The glutaredoxins do not act as enzymes, but rather as a cofactor, enabling intracellular redox reactions through
a disulfide/dithiol enzymatic mechanism involving the active site cysteines.
There is almost no similarity between the amino acid sequence of Grx2 (an approximately 27 kDa protein) and Grx1
or Grx3 (both 9-kDa proteins), with the exception of the active site which is identical in all three glutaredoxins.
In contrast to glutaredoxin 1 and 3, Grx 2 is not a hydrogen donor for ribonucleotide reductase.
On the other hand, Grx2 is the primary hydrogen donor to ArsC-catalyzed arsenate reduction (|FRAME: RXN-982|)
|CITS: [10593884]|. It is also the most abundant glutaredoxin in the cell, with an intracellular concentration
of 5 µM, compared with 0.2 µM and 2.4 µM for Grx1 and 3, respectively |CITS: [10593884]|.)""",
('B1064', 'GRXR') : """(Glutaredoxins are ubiquitous proteins that catalyze the reduction of disulfides via reduced glutathione (GSH).
Escherichia coli has three glutaredoxins (Grx1, Grx2, and Grx3) containing the classic dithiol active site
CPYC, and a fourth one which contains a monothiol (CGFS) potential active site |CITS: [15833738]|.
The glutaredoxins do not act as enzymes, but rather as a cofactor, enabling intracellular redox reactions through
a disulfide/dithiol enzymatic mechanism involving the active site cysteines.
There is almost no similarity between the amino acid sequence of Grx2 (an approximately 27 kDa protein) and Grx1
or Grx3 (both 9-kDa proteins), with the exception of the active site which is identical in all three glutaredoxins.
In contrast to glutaredoxin 1 and 3, Grx 2 is not a hydrogen donor for ribonucleotide reductase.
On the other hand, Grx2 is the primary hydrogen donor to ArsC-catalyzed arsenate reduction (|FRAME: RXN-982|)
|CITS: [10593884]|. It is also the most abundant glutaredoxin in the cell, with an intracellular concentration
of 5 µM, compared with 0.2 µM and 2.4 µM for Grx1 and 3, respectively |CITS: [10593884]|.)""",
('B3610', 'GRXR') : """(There at least three glutaredoxins in E. coli. Glutaredoxin
3 is able to function as a disulfide reductase, but not as well as
glutaredoxin 1. Coupled with cellular glutathione it may be the third
hydrogen donor system in the absence of thioredoxin and glutaredoxin
1. Under normal conditions it is likely that glutaredoxin has other
functions. |CITS: [95024051] [96215095]|)""",
('B3610', 'GRXR') : """NIL""",
('B0849', 'GRXR') : """NIL""",
('B0849', 'GRXR') : """(Glutaredoxins are ubiquitous proteins that catalyze the reduction of disulfides via reduced glutathione (GSH).
Escherichia coli has three glutaredoxins (Grx1, Grx2, and Grx3) containing the classic dithiol active site
CPYC, and a fourth one which contains a monothiol (CGFS) potential active site |CITS: [15833738]|.
The glutaredoxins act as a cofactor enabling intracellular redox reactions through a disulfide/dithiol
enzymatic mechanism involving the active site cysteines. They are used as a
hydrogen donor for the glutathione(GSH)-dependent synthesis of deoxyribonucleotides
by ribonucleotide reductase and reduces specific cysteine residues in
ribonucleotide reductase.
Glutaredoxin are also a hydrogen donor for the reduction of adenosine 3'-phosphate 5'-phosphosulfate
and methionine sulfoxide.
In addition, glutaredoxins also catalyzes GSH-disulfide oxidoreduction reactions with low molecular weight
substrates. |CITS: [79151138] [91242463] [93003075]| There are two additional
glutaredoxins in E. coli whose physiological roles have not been fully
determined. |CITS: [95024051]|)""",
('B1654', 'GRXR') : """(Grx4 belongs to the family of monothiol glutaredoxins. Oxidized Grx4 can be reduced by the thioredoxin system or
glutaredoxin 1. Grx4 is not active in the standard glutaredoxin assay |CITS: [15833738]|.
Grx4 is an abundant protein that is upregulated during stationary phase; the increased expression is dependent on
ppGpp |CITS: [15833738]|.
A grxD null mutant could not be obtained |CITS: [15833738]|. grxD has previously been reported to be
essential for aerobic growth in rich media |CITS: [13129938]|.
A solution structure of the reduced form of Grx4 has been determined |CITS: [15840565]|)""",
('B4407', 'THZPSN') : """(ThiS is the sulfur source for the thiazole moiety in thiamin
biosynthesis. In a reaction catalyzed by the ThiF protein, ThiS is
adenylated, yielding ThiS-COAMP. Sulfur is transferred to ThiS-COAMP
from cysteine in a reaction also catalyzed by ThiF and the ThiI protein, yielding
ThiS-COSH. |CITS: [99311269] [98298179]|)""",
('B4407', 'THZPSN') : """(ThiS is the sulfur source for the thiazole moiety in thiamin
biosynthesis. In a reaction catalyzed by the ThiF protein, ThiS is
adenylated, yielding ThiS-COAMP. Sulfur is transferred to ThiS-COAMP
from cysteine in a reaction also catalyzed by ThiF and the ThiI protein, yielding
ThiS-COSH. In a reaction combining deoxy-D-xylulose-P, tyrosine and
ThiS-COSH the thiazole moiety is synthesized. |CITS: [99311269] [98298179]|)""",
('B4407', 'THZPSN') : """(ThiS is the sulfur source for the thiazole moiety in thiamin
biosynthesis. In a reaction catalyzed by the ThiF protein, ThiS is
adenylated, yielding ThiS-COAMP. Sulfur is transferred to ThiS-COAMP
from cysteine in a reaction also catalyzed by ThiF and the ThiI protein, yielding
ThiS-COSH. |CITS: [99311269] [98298179]|)""",
('B3622', 'O16A4Lpp') : """(The lipopolysaccharide of E. coli K-12 consists of two major components:
the hydrophobic lipid A moiety inserted into the outer membrane and the
phosphorylated core oligosaccharide |CITS:[12045108]|. E. coli K-12
does not produce O antigen to attach to the LPS core due to a defect in the
rfb gene cluster which can be complemented with genes from a second,
independent rfb mutant to produce an O16 type O antigen |CITS:[7517391]|.
E. coli K-12 may have two major pathways for LPS biosynthesis. One
generates LPS cores suitable for O antigen attachment, and a second generates
lipooligosaccharides (LOS) with modifications to the core structure which prevent
O antigen attachment |CITS:[1385388]|.
WaaL is thought to be the O-antigen ligase in the lipopolysaccharide synthesis pathway.
Unlike most LPS core
biosynthesis genes, waaL has little sequence similarity to the counterpart gene in Salmonella
enterica
|CITS: [1624462]|. This diversity is thought to play a role in generating core specificity and
species-specific
attachment of O antigen |CITS: [1385388]|. WaaL may function together with WaaU |CITS: [9535865]|.
Both WaaU and WaaL are required for the complementation of a waaK mutation in
S. typhimurium LT2, suggesting an interaction between the two proteins |CITS:[1385388]|.
WaaL is an inner membrane protein with 12 predicted membrane-spanning regions. Its C terminus is located in the
cytoplasm |CITS: [15919996]|.
Inactivation of waaL does not cause a detectable
morphological phenotype; this is not surprising, because the
K-12 strain lacks the O antigen |CITS: [1577693]|.
However, waaL appears to be required for core completion
|CITS: [1385388]|. A waaL mutant prevents core completion
by rfp of Shigella dysenteriae 1, suggesting its own
role in core completion |CITS:[1385388]|.
Reviews: |CITS:[12045108],[9157235],[9791168],[7504166]|)""",
('B0936', 'ISETACabcpp') : """NIL""",
('B0936', 'ISETACabcpp') : """(Deletion mutation studies |CITS:[10506196]| indicate that the ssuEADCB gene cluster codes for proteins that enable Escherichia coli
to utilize sulfonates other than taurine as a sulfur source. Based on sequence similarity SsuABC is the ABC type transport system with
SsuA being the periplasmic substrate-binding subunit, SsuB the ATP-binding subunit and SsuC the permease. ssuD and
ssuE encode an FMNH2-dependent monooxygenase and an NAD(P)H-dependent FMN reductase, respectively.)""",
('B0933', 'ISETACabcpp') : """(ATP-binding component of ABC transporter)""",
('B0933', 'ISETACabcpp') : """(Deletion mutation studies |CITS:[10506196]| indicate that the ssuEADCB gene cluster codes for proteins that enable Escherichia coli
to utilize sulfonates other than taurine as a sulfur source. Based on sequence similarity SsuABC is the ABC type transport system with
SsuA being the periplasmic substrate-binding subunit, SsuB the ATP-binding subunit and SsuC the permease. ssuD and
ssuE encode an FMNH2-dependent monooxygenase and an NAD(P)H-dependent FMN reductase, respectively.)""",
('B0934', 'ISETACabcpp') : """(membrane component of ABC transporter
Protein topology in the inner membrane has been determined |CITS: [11867724]|.)""",
('B0934', 'ISETACabcpp') : """(Deletion mutation studies |CITS:[10506196]| indicate that the ssuEADCB gene cluster codes for proteins that enable Escherichia coli
to utilize sulfonates other than taurine as a sulfur source. Based on sequence similarity SsuABC is the ABC type transport system with
SsuA being the periplasmic substrate-binding subunit, SsuB the ATP-binding subunit and SsuC the permease. ssuD and
ssuE encode an FMNH2-dependent monooxygenase and an NAD(P)H-dependent FMN reductase, respectively.)""",
('B3370', 'FRULYSt2pp') : """(FrlA is an uncharacterized member of the APC superfamily of amino acid transporters |CITS:[20391827]|. Based on
the activities of FrlB and FrlD, FrlA is suggested to transport fructoselysine, which can be utilized as a carbon source
|CITS: [12147680]|. The function of FrlA has not been experimentally determined.
An frlA mutant is unable to grow on 20mM fructoselysine or psicoselysine as the sole source of carbon
|CITS: [14641112]|.
FrlA: "fructoselysine" |CITS: [12147680]|.)""",
('B0684', 'RNTR4c') : """(Flavodoxins are small, acidic electron transfer proteins which contain FMN as a prosthetic group. They are only
able to accept and donate electrons. Flavodoxin is an important member of the multi-enzyme complexes that are
involved in the activation of anaerobic nucleoside reductase and pyruvate-formate lyase. Flavodoxins are
functionally interchangeable with ferredoxins, but some enzymes are specific for one or the other. E. coli has
at least two flavodoxins |CITS: [91154129][95050480][93194782]|.
FldA is essential under both aerobic and anaerobic growth conditions |CITS: [10714981]|. The essential role for
flavodoxin 1 under aerobic conditions is in the MEP pathway for isoprenoid biosynthesis
(|FRAME: NONMEVIPP-PWY|) |CITS: [15978585]|.
Crystal and solution structures of FldA have been solved |CITS: [9416602][9119004]|.)""",
('B0684', 'RNTR4c') : """NIL""",
('B2895', 'RNTR4c') : """(Flavodoxins are small, acidic electron transfer proteins
which contain FMN as a prosthetic group. They are only able to accept
and donate electrons. Flavodoxin is an important member of the
multi-enzyme complexes that are involved in the activation of
anaerobic nucleoside reductase and pyruvate-formate lyase. Flavodoxins
are functionally interchangeable with ferredoxins but some enzymes are
specific for one or the other. E. coli has at least two flavodoxins.
|CITS: [91154129] [95050480] [93194782]|)""",
('B2895', 'RNTR4c') : """NIL""",
('B0684', 'RNTR4c') : """(Flavodoxins are small, acidic electron transfer proteins which contain FMN as a prosthetic group. They are only
able to accept and donate electrons. Flavodoxin is an important member of the multi-enzyme complexes that are
involved in the activation of anaerobic nucleoside reductase and pyruvate-formate lyase. Flavodoxins are
functionally interchangeable with ferredoxins, but some enzymes are specific for one or the other. E. coli has
at least two flavodoxins |CITS: [91154129][95050480][93194782]|.
FldA is essential under both aerobic and anaerobic growth conditions |CITS: [10714981]|. The essential role for
flavodoxin 1 under aerobic conditions is in the MEP pathway for isoprenoid biosynthesis
(|FRAME: NONMEVIPP-PWY|) |CITS: [15978585]|.
Crystal and solution structures of FldA have been solved |CITS: [9416602][9119004]|.)""",
('B0684', 'RNTR4c') : """NIL""",
('B2895', 'RNTR4c') : """(Flavodoxins are small, acidic electron transfer proteins
which contain FMN as a prosthetic group. They are only able to accept
and donate electrons. Flavodoxin is an important member of the
multi-enzyme complexes that are involved in the activation of
anaerobic nucleoside reductase and pyruvate-formate lyase. Flavodoxins
are functionally interchangeable with ferredoxins but some enzymes are
specific for one or the other. E. coli has at least two flavodoxins.
|CITS: [91154129] [95050480] [93194782]|)""",
('B2895', 'RNTR4c') : """NIL""",
('B1801', 'GLYt2pp') : """(YeaV is an uncharacterized member of the Betaine, Carnitine, Choline Transporter (BCCT)
family |CITS:[95115548]|. Based on bioinformatic analysis, YeaV shows highest amino acid sequence
similarity with carnitine transporters.)""",
('B2835', '2AGPA141tipp') : """(LplT is a major facilitator superfamily (MFS) protein that acts as a flippase for transbilayer movement of
lysophospholipids. Mutation experiments and
transporter assays have determined LplT is responsible for the facilitated diffusion of lysophospholipids to
the cytoplasmic portion of the inner membrane providing substrate for the bifunctional enzyme
2-acyl-GPE acyltransferase/acyl-ACP synthetase (Aas). lplT forms an operon with the aas
gene |CITS:[15661733]|.)""",
('B0684', 'RNTR1c') : """(Flavodoxins are small, acidic electron transfer proteins which contain FMN as a prosthetic group. They are only
able to accept and donate electrons. Flavodoxin is an important member of the multi-enzyme complexes that are
involved in the activation of anaerobic nucleoside reductase and pyruvate-formate lyase. Flavodoxins are
functionally interchangeable with ferredoxins, but some enzymes are specific for one or the other. E. coli has
at least two flavodoxins |CITS: [91154129][95050480][93194782]|.
FldA is essential under both aerobic and anaerobic growth conditions |CITS: [10714981]|. The essential role for
flavodoxin 1 under aerobic conditions is in the MEP pathway for isoprenoid biosynthesis
(|FRAME: NONMEVIPP-PWY|) |CITS: [15978585]|.
Crystal and solution structures of FldA have been solved |CITS: [9416602][9119004]|.)""",
('B0684', 'RNTR1c') : """NIL""",
('B0684', 'RNTR1c') : """(Flavodoxins are small, acidic electron transfer proteins which contain FMN as a prosthetic group. They are only
able to accept and donate electrons. Flavodoxin is an important member of the multi-enzyme complexes that are
involved in the activation of anaerobic nucleoside reductase and pyruvate-formate lyase. Flavodoxins are
functionally interchangeable with ferredoxins, but some enzymes are specific for one or the other. E. coli has
at least two flavodoxins |CITS: [91154129][95050480][93194782]|.
FldA is essential under both aerobic and anaerobic growth conditions |CITS: [10714981]|. The essential role for
flavodoxin 1 under aerobic conditions is in the MEP pathway for isoprenoid biosynthesis
(|FRAME: NONMEVIPP-PWY|) |CITS: [15978585]|.
Crystal and solution structures of FldA have been solved |CITS: [9416602][9119004]|.)""",
('B0684', 'RNTR1c') : """NIL""",
('B2895', 'RNTR1c') : """(Flavodoxins are small, acidic electron transfer proteins
which contain FMN as a prosthetic group. They are only able to accept
and donate electrons. Flavodoxin is an important member of the
multi-enzyme complexes that are involved in the activation of
anaerobic nucleoside reductase and pyruvate-formate lyase. Flavodoxins
are functionally interchangeable with ferredoxins but some enzymes are
specific for one or the other. E. coli has at least two flavodoxins.
|CITS: [91154129] [95050480] [93194782]|)""",
('B2895', 'RNTR1c') : """NIL""",
('B2895', 'RNTR1c') : """(Flavodoxins are small, acidic electron transfer proteins
which contain FMN as a prosthetic group. They are only able to accept
and donate electrons. Flavodoxin is an important member of the
multi-enzyme complexes that are involved in the activation of
anaerobic nucleoside reductase and pyruvate-formate lyase. Flavodoxins
are functionally interchangeable with ferredoxins but some enzymes are
specific for one or the other. E. coli has at least two flavodoxins.
|CITS: [91154129] [95050480] [93194782]|)""",
('B2895', 'RNTR1c') : """NIL""",
('B2582', 'PAPSR') : """(The trxC gene encodes a second thioredoxin in E. coli. Thioredoxin 2 can perform many of
thioredoxin 1's roles in vivo; it is able to reduce some essential cytoplasmic enzymes.
Along with thioredoxin 1 and glutaredoxin 1, thioredoxin 2 is one of E. coli's most
effective cytoplasmic disulfide-reducing proteins. Any one of these three is sufficient
to support aerobic growth. |CITS: [98429478] [98049550]|)""",
('B2582', 'PAPSR') : """NIL""",
('B3781', 'PAPSR') : """(Thioredoxin is a small electron-transfer protein which contains a cysteine
disulfide/dithiol active site. The protein functions in a wide variety of cellular
processes. Thioredoxin is reduced by NADPH in a reaction catalyzed by
thioredoxin reductase. The conversion between the oxidized and reduced
forms results in a change of conformation. The functional properties differ
between the two forms of thioredoxin. The reduced thioredoxin is a powerful
protein disulfide reductase, thioredoxin catalyzes dithiol-disulfide exchange
reactions. The oxidized form of thioredoxin has been crystallized,
the reduced form has been solved by NMR. |CITS: [85277988] [90198521]
[90254096] [90298180] [93264420] [90204538]|)""",
('B3781', 'PAPSR') : """(Thioredoxin is a small electron-transfer protein which contains a cysteine
disulfide/dithiol active site. The protein functions in a wide variety of cellular
processes. Thioredoxin is reduced by NADPH in a reaction catalyzed by
thioredoxin reductase. The conversion between the oxidized and reduced
forms results in a change of conformation. The functional properties differ
between the two forms of thioredoxin. The reduced thioredoxin is a powerful
protein disulfide reductase, thioredoxin catalyzes dithiol-disulfide exchange
reactions. The oxidized form of thioredoxin has been crystallized, the reduced
form has been solved by NMR.
|CITS: [85277988] [90198521] [90254096] [90298180] [93264420] [90204538]|)""",
('B1621', 'GLCptspp') : """(contains PTS Enzyme IIB and IIC domains)""",
('B1621', 'GLCptspp') : """(MalX, the maltose-glucose PTS permease, belongs to the functional
superfamily of the phosphoenolpyruvate (PEP)-dependent, sugar
transporting phosphotransferase system (PTS). The PTS transports
and simultaneously phosphorylates its sugar substrates in a process
called group translocation. MalX presumably takes up exogenous
sugar, releasing the phosphate ester into the cell cytoplasm in
preparation for metabolism |CITS: [8246840]|. The overall PTS-mediated phosphoryl
transfer reaction, requiring the two general energy coupling proteins
of the PTS, Enzyme I and HPr, as well as the three domains of
the Enzyme II complex is:
PEP --> Enzyme I(his~~P)
--> HPr(his~~P)
--> IIA(his~~P) -->
IIB(cys~~P) -(IIC)-> sugar-P.
The MalX (Enzyme IICBMal) can use glucose
and maltose as substrates. It may catalyze facilitated diffusion
as well as group translocation |CITS: [1856179]| . The protein presumably functions
with the glucose Enzyme IIA and is homologous to the glucose-
and N-acetylglucosamine-specific Enzyme IICBs. The physiological
function of MalX is not known |CITS: [1856179]|.
)""",
('B0657', 'ALPATG160pp') : """(Apolipoprotein N-acyltransferase activity transfers palmitate to apolipoproteins, resulting in the maturation of lipoproteins from apolipoprotein precursors |CITS: [2032623]|. Aminoacylation of lipoproteins bound for the outer membrane is required for proper localization of these lipoproteins via the Lol pathway |CITS: [12198129]|.
The enzyme activity has been characterized |CITS: [2032623]|. The enzyme can utilize the phospholipids phosphatidylethanolamine, phosphatidylglycerol, or cardiolipin in vitro |CITS: [2032623]|. A pss mutant exhibits apolipoprotein N-acyltransferase activity, indicating that the enzyme is not specific for a phosphatidylethanolamine donor in vivo |CITS: [2033085]|.
Apolipoprotein N-acyltransferase localizes to inner membrane or inner-plus-outer membrane fractions |CITS: [2032623]|.
A cutE mutant exhibits copper sensitivity |CITS: [1938881]|.
CutE has a region with similarity to copper binding sites |CITS: [1938881]|.
CutE functionally complements the heat sensitivity, copper sensitivity, and apolipoprotein N-acyltransferase defect of a Salmonella typhimurium SE5312 mutant |CITS: [8344936]|. CutE overproduction in Salmonella typhimurium results in increased apolipoprotein N-acyltransferase activity |CITS: [8344936]|.
CutE has similarity to Rhizobium meliloti ActA |CITS: [8868435]|.
Regulation has been described |CITS: [1938881]|.
Review: |CITS: [7651187]|.)""",
('B1677', 'ALPATG160pp') : """(Lpp, the major lipoprotein, is one of the most abundant proteins in Escherichia coli |CITS:[4610570]| and is
necessary for the stabilization and integrity of the bacterial cell envelope |CITS:[11790745]|. The three-dimensional crystal structure of Lpp has been determined to 1.9 A resolution |CITS:[10843861]|. Cells lacking Lpp or with mutations affecting the attachment of Lpp to the murein (peptidoglycan) layer exhibit outer membrane blebs, are hypersensitive to toxic compounds, and release periplasmic proteins to the extracellular medium |CITS:[105245]|. Lpp exists in two forms, a free form and a covalently linked bound form attached to the peptidoglycan. Both forms are localized to the outer membrane |CITS:[4245367]|, |CITS:[4565677]|. Lpp is expressed as a prolipoprotein, having 20 amino acid residues extending from the amino terminus |CITS:[322142]| During translocation across the cytoplasmic membrane, the prolipoprotein undergoes modifications of the amino terminus cysteine residue followed by cleavage of the signal peptide extension |CITS:[8051048]|. The mature lipoprotein is then translocated to the outer membrane where it is covalently bound to the peptidoglycan layer |CITS:[6369111]|, |CITS:[6363408]|. Globomycin was found to inhibit the cleavage by signal peptidase II through noncompetitive binding to the enzyme |CITS:[3888977]|. Studies using inhibitors of the proton motive force (pmf) and ATP-depleted cells indicated that both the pmf and ATP are required for translocation of an OmpF-Lpp chimeric protein |CITS:[3029075]|. Translocation across the inner membrane was found to involve the Sec export apparatus |CITS:[2842297]|. Immunoelectron microscopy revealed that free lipoprotein is inserted equally over the entire cell wall, that lipoprotein synthesis increases with cell length, and that cell shape depends on total lipoprotein content of the cell in that low total lipoprotein corresponds to a spherical shape and a higher lipoprotein content corresponds with a rod shape |CITS:[3316185]|. Pulse-chase labeling followed by cell fractionation found that Lpp utilizes the LolA-LolB system to facilitate its release from the inner membrane and localization to the outer membrane |CITS:[10521496]|. Chemical cross-linking has revealed that Lpp organizes into trimers and interacts with OmpA, a major outer membrane lipoprotein |CITS:[3013869]|.)""",
('B3127', 'GLCRt2rpp') : """(YhaU is an uncharacterised member of the major facilitator superfamily (MFS)
of transporters |CITS: [98190790]|.
Based on sequence similarity, YhaU may function as a proton-driven
glucarate uptake system.)""",
('B2789', 'GLCRt2rpp') : """(The YgcZ protein may function as a glucarate transporter. The
ygcZ gene is encoded in a probable operon with genes
encoding two subunits of a putative glucarate dehydratase. YgcZ
is a member of the major facilitator superfamily (MFS) of
transporters |CITS: [98190790]| and shares a high level of sequence
similarity with probable glucarate transporters from various
organisms. YgcZ probably functions as a glucarate/proton transporter.)""",
('B2835', '2AGPA181tipp') : """(LplT is a major facilitator superfamily (MFS) protein that acts as a flippase for transbilayer movement of
lysophospholipids. Mutation experiments and
transporter assays have determined LplT is responsible for the facilitated diffusion of lysophospholipids to
the cytoplasmic portion of the inner membrane providing substrate for the bifunctional enzyme
2-acyl-GPE acyltransferase/acyl-ACP synthetase (Aas). lplT forms an operon with the aas
gene |CITS:[15661733]|.)""",
('B3370', 'PSCLYSt2pp') : """(FrlA is an uncharacterized member of the APC superfamily of amino acid transporters |CITS:[20391827]|. Based on
the activities of FrlB and FrlD, FrlA is suggested to transport fructoselysine, which can be utilized as a carbon source
|CITS: [12147680]|. The function of FrlA has not been experimentally determined.
An frlA mutant is unable to grow on 20mM fructoselysine or psicoselysine as the sole source of carbon
|CITS: [14641112]|.
FrlA: "fructoselysine" |CITS: [12147680]|.)""",
('B2835', '2AGPG140tipp') : """(LplT is a major facilitator superfamily (MFS) protein that acts as a flippase for transbilayer movement of
lysophospholipids. Mutation experiments and
transporter assays have determined LplT is responsible for the facilitated diffusion of lysophospholipids to
the cytoplasmic portion of the inner membrane providing substrate for the bifunctional enzyme
2-acyl-GPE acyltransferase/acyl-ACP synthetase (Aas). lplT forms an operon with the aas
gene |CITS:[15661733]|.)""",
('B3396', 'MPTG') : """(PBP1A is the product of the mrcA gene |CITS:[3882429]|. PBP1A is a bifunctional, inner membrane enzyme
catalyzing the transglycosylation and transpeptidation of murein (peptidoglycan) precursors in the formation of the
murein sacculus |CITS:[9529891]|. The amino terminus contains a signal sequence |CITS:[3882429]|. PBP1A is able
to dimerize without disulfide bonds, but doesn't form a complex with PBP1B |CITS:[12057973]|. Either PBP1A or
PBP1B (the other major bifunctional enzyme in murein synthesis with a different penicillin-binding affinity) is required
for cell elongation because a PBP1A-PBP1B double mutation is lethal |CITS:[1103132][341159][345275][2993822]|.
Experiments have been performed involving inhibition or mutation of PBP1A alone or coupled with inhibition or
mutation of other proteins involved in cell division and murein metabolism |CITS:[7007327][2211517][2066344][10383966]|.)""",
('B2519', 'MPTG') : """(The PbpC protein contains both a penicillin-binding and a transglycosylase domain. Deletion of the pbpC gene
does not cause an obvious phenotype, and overproduction of the PbpC protein does not rescue the defect of a
ponAts ponB double mutant |CITS: [10542235]|.
PbpC interacts with PBP1B, PBP3, and MltA |CITS: [10542235]|.)""",
('B4301', 'RPE') : """(No information about this protein was found by a literature search conducted on September 19, 2005.)""",
('B1094', 'MCOATA') : """(Acyl carrier protein (ACP) plays an important role in fatty
acid biosynthesis. It carries fatty acid chains via a thioester
linkage to a phosphopantetheine prosthetic group as the chains are
elongated. There is also evidence that it has a function in the
biosynthesis of membrane-derived oligosaccharides. Therefore ACP and
its acyl forms interact with at least 12 different E. coli enzymes.
|CITS: [92210530] [89050961] [88296479]| ACP is the most abundant
protein in E. coli, with about 1.5E6 molecules per cell. |CITS: [Mathews&vanHolde]| ACP contains a
phosphopantetheine moiety (as does CoA) as the reactive unit, attached
to the ACP protein through a serine. The holo-ACP synthase enzyme
(encoded by the acpS gene) transfers the 4-phosphopantetheine
moeity of CoA to the apo-ACP to form holo-ACP, which is the active
form of the carrier in lipid synthesis |CITS: [68313114] [81215492]|.)""",
('B1094', 'MCOATA') : """(Lipoate synthase catalyzes the step of lipoic acid biosynthesis at which sulfur is inserted into octanoyl-ACP to form the lipoate moiety |CITS: [8444795], [11106496]|. Lipoate modification (by lipoyl-protein ligases LipB or LplA) of complex subunits is important for function of pyruvate dehydrogenase |CITS: [814874], [6794598], [8444795]|, alpha-ketoglutarate dehydrogenase |CITS: [814874], [6794598], [8444795]|, and the glycine cleavage system |CITS: [1655709], [8444795]|.)""",
('B1094', 'MCOATA') : """(Lipoate synthase catalyzes the step of lipoic acid biosynthesis at which sulfur is inserted into octanoyl-ACP to form the lipoate moiety |CITS: [8444795], [11106496]|. Lipoate synthase is a LipA homodimer with two (4Fe-4S) iron-sulfur clusters per protein dimer under anaerobic conditions, and these clusters are oxidized to the (2Fe-2S) state in air |CITS: [10747808], [10403368]|. The enzyme uses octanoyl-ACP, but not octanoic acid, as substrate and also uses S-adenosyl methionine |CITS: [11106496]|.)""",
('B1094', 'MCOATA') : """NIL""",
('B1094', 'MCOATA') : """NIL""",
('B1094', 'MCOATA') : """NIL""",
('B1094', 'MCOATA') : """NIL""",
('B1094', 'MCOATA') : """NIL""",
('B1094', 'MCOATA') : """NIL""",
('B1094', 'MCOATA') : """NIL""",
('B1094', 'MCOATA') : """NIL""",
('B1094', 'MCOATA') : """NIL""",
('B1094', 'MCOATA') : """NIL""",
('B1094', 'MCOATA') : """NIL""",
('B1094', 'MCOATA') : """NIL""",
('B1094', 'MCOATA') : """NIL""",
('B1094', 'MCOATA') : """NIL""",
('B1094', 'MCOATA') : """NIL""",
('B1094', 'MCOATA') : """NIL""",
('B1094', 'MCOATA') : """(The holo-ACP synthase enzyme (encoded by acpS) transfers the 4-phosphopantetheine
moiety of CoA to the apo-ACP to form holo-ACP, which is the active
form of the carrier in lipid synthesis |CITS: [68313114] [81215492]|.)""",
('B3469', 'HG2abcpp') : """(The gene product of the yhhO gene, also referred to as zntA, is
a P-type ATPase involved in the efflux of Pb(II), Cd(II), and Zn(II) |CITS:[98070750] [20263730]|.
ZntA displays a Km of approximately 20 μM for Cd(II) and
100 μM for Zn(II) |CITS:[20127859]|. The transporter appears to be inhibited
by vanadate, a common inhibitor of P-type ATPase. The ATPase activity of the
transporter was found to follow the order Pb(II), Cd(II), Zn(II), and Hg(II) |CITS:[20127859]|.
A zntA mutant showed hypersensitivity to Cd(II) and Zn(II) |CITS:[98070750]|.
The zntA gene was found to be under the control of the transcriptional
regulator ZntR. zntA expression is activated by an increased concentration
of Cd(II) and Zn(II) within the cell, showing greater induction by Cd(II) than by
Zn(II) |CITS:[20127859]|.)""",
('B2923', 'LYSt3pp') : """(The ArgO (YggA) protein is a member of the LysE family of lysine efflux transporters |CITS: [99257453]|.
Based on sequence similarity, ArgO may function as a proton-driven amino acid efflux system.
Null mutations in both the argO and the argP genes cause hypersensitivity to canavanine, an arginine analog. ArgO
expression is regulated by ArgP, and transcription of argO is induced by exogenous arginine |CITS: [15150242]|.
ArgO = "arginine outward transport" |CITS: [15150242]|)""",
('B0411', 'DADNtex') : """(Tsx is a protein involved with the permeation of ribo- and deoxy-nucleosides, across the outer membrane of E. coli.
It also allows the entry of the antibiotic albicidin, and serves as a receptor for bacteriophage and colicins |CITS: [3276691]|
It is believed to form a 14 strand β-barrel porin.
The crystal structure of Tsx has been determined up to 3.1 A co-crystallized with a range of nucleosides |CITS:[15272310]|. Tsx has been shown to localize to the cellular poles |CITS:[15130122]|.)""",
('B0511', 'ALLTNt2rpp') : """(The YbbW protein is an uncharacterized member of the
NCS1 family of purine and pyrimidine transporters
|CITS: [99184734]|. Based on sequence similarity,
YbbW may function as a proton-driven allantoin uptake
system. Supporting this notion, the downstream gene
from ybbW encodes a putative allantoinase enzyme.)""",
('B3469', 'CU2abcpp') : """(The gene product of the yhhO gene, also referred to as zntA, is
a P-type ATPase involved in the efflux of Pb(II), Cd(II), and Zn(II) |CITS:[98070750] [20263730]|.
ZntA displays a Km of approximately 20 μM for Cd(II) and
100 μM for Zn(II) |CITS:[20127859]|. The transporter appears to be inhibited
by vanadate, a common inhibitor of P-type ATPase. The ATPase activity of the
transporter was found to follow the order Pb(II), Cd(II), Zn(II), and Hg(II) |CITS:[20127859]|.
A zntA mutant showed hypersensitivity to Cd(II) and Zn(II) |CITS:[98070750]|.
The zntA gene was found to be under the control of the transcriptional
regulator ZntR. zntA expression is activated by an increased concentration
of Cd(II) and Zn(II) within the cell, showing greater induction by Cd(II) than by
Zn(II) |CITS:[20127859]|.)""",
('B2923', 'ARGt3pp') : """(The ArgO (YggA) protein is a member of the LysE family of lysine efflux transporters |CITS: [99257453]|.
Based on sequence similarity, ArgO may function as a proton-driven amino acid efflux system.
Null mutations in both the argO and the argP genes cause hypersensitivity to canavanine, an arginine analog. ArgO
expression is regulated by ArgP, and transcription of argO is induced by exogenous arginine |CITS: [15150242]|.
ArgO = "arginine outward transport" |CITS: [15150242]|)""",
('B0849', 'PAPSR2') : """NIL""",
('B0849', 'PAPSR2') : """(Glutaredoxins are ubiquitous proteins that catalyze the reduction of disulfides via reduced glutathione (GSH).
Escherichia coli has three glutaredoxins (Grx1, Grx2, and Grx3) containing the classic dithiol active site
CPYC, and a fourth one which contains a monothiol (CGFS) potential active site |CITS: [15833738]|.
The glutaredoxins act as a cofactor enabling intracellular redox reactions through a disulfide/dithiol
enzymatic mechanism involving the active site cysteines. They are used as a
hydrogen donor for the glutathione(GSH)-dependent synthesis of deoxyribonucleotides
by ribonucleotide reductase and reduces specific cysteine residues in
ribonucleotide reductase.
Glutaredoxin are also a hydrogen donor for the reduction of adenosine 3'-phosphate 5'-phosphosulfate
and methionine sulfoxide.
In addition, glutaredoxins also catalyzes GSH-disulfide oxidoreduction reactions with low molecular weight
substrates. |CITS: [79151138] [91242463] [93003075]| There are two additional
glutaredoxins in E. coli whose physiological roles have not been fully
determined. |CITS: [95024051]|)""",
('B1064', 'PAPSR2') : """(Glutaredoxins are ubiquitous proteins that catalyze the reduction of disulfides via reduced glutathione (GSH).
Escherichia coli has three glutaredoxins (Grx1, Grx2, and Grx3) containing the classic dithiol active site
CPYC, and a fourth one which contains a monothiol (CGFS) potential active site |CITS: [15833738]|.
The glutaredoxins do not act as enzymes, but rather as a cofactor, enabling intracellular redox reactions through
a disulfide/dithiol enzymatic mechanism involving the active site cysteines.
There is almost no similarity between the amino acid sequence of Grx2 (an approximately 27 kDa protein) and Grx1
or Grx3 (both 9-kDa proteins), with the exception of the active site which is identical in all three glutaredoxins.
In contrast to glutaredoxin 1 and 3, Grx 2 is not a hydrogen donor for ribonucleotide reductase.
On the other hand, Grx2 is the primary hydrogen donor to ArsC-catalyzed arsenate reduction (|FRAME: RXN-982|)
|CITS: [10593884]|. It is also the most abundant glutaredoxin in the cell, with an intracellular concentration
of 5 µM, compared with 0.2 µM and 2.4 µM for Grx1 and 3, respectively |CITS: [10593884]|.)""",
('B1064', 'PAPSR2') : """(Glutaredoxins are ubiquitous proteins that catalyze the reduction of disulfides via reduced glutathione (GSH).
Escherichia coli has three glutaredoxins (Grx1, Grx2, and Grx3) containing the classic dithiol active site
CPYC, and a fourth one which contains a monothiol (CGFS) potential active site |CITS: [15833738]|.
The glutaredoxins do not act as enzymes, but rather as a cofactor, enabling intracellular redox reactions through
a disulfide/dithiol enzymatic mechanism involving the active site cysteines.
There is almost no similarity between the amino acid sequence of Grx2 (an approximately 27 kDa protein) and Grx1
or Grx3 (both 9-kDa proteins), with the exception of the active site which is identical in all three glutaredoxins.
In contrast to glutaredoxin 1 and 3, Grx 2 is not a hydrogen donor for ribonucleotide reductase.
On the other hand, Grx2 is the primary hydrogen donor to ArsC-catalyzed arsenate reduction (|FRAME: RXN-982|)
|CITS: [10593884]|. It is also the most abundant glutaredoxin in the cell, with an intracellular concentration
of 5 µM, compared with 0.2 µM and 2.4 µM for Grx1 and 3, respectively |CITS: [10593884]|.)""",
('B1654', 'PAPSR2') : """(Grx4 belongs to the family of monothiol glutaredoxins. Oxidized Grx4 can be reduced by the thioredoxin system or
glutaredoxin 1. Grx4 is not active in the standard glutaredoxin assay |CITS: [15833738]|.
Grx4 is an abundant protein that is upregulated during stationary phase; the increased expression is dependent on
ppGpp |CITS: [15833738]|.
A grxD null mutant could not be obtained |CITS: [15833738]|. grxD has previously been reported to be
essential for aerobic growth in rich media |CITS: [13129938]|.
A solution structure of the reduced form of Grx4 has been determined |CITS: [15840565]|)""",
('B3610', 'PAPSR2') : """(There at least three glutaredoxins in E. coli. Glutaredoxin
3 is able to function as a disulfide reductase, but not as well as
glutaredoxin 1. Coupled with cellular glutathione it may be the third
hydrogen donor system in the absence of thioredoxin and glutaredoxin
1. Under normal conditions it is likely that glutaredoxin has other
functions. |CITS: [95024051] [96215095]|)""",
('B3610', 'PAPSR2') : """NIL""",
('B3781', 'THIORDXi') : """(Thioredoxin is a small electron-transfer protein which contains a cysteine
disulfide/dithiol active site. The protein functions in a wide variety of cellular
processes. Thioredoxin is reduced by NADPH in a reaction catalyzed by
thioredoxin reductase. The conversion between the oxidized and reduced
forms results in a change of conformation. The functional properties differ
between the two forms of thioredoxin. The reduced thioredoxin is a powerful
protein disulfide reductase, thioredoxin catalyzes dithiol-disulfide exchange
reactions. The oxidized form of thioredoxin has been crystallized,
the reduced form has been solved by NMR. |CITS: [85277988] [90198521]
[90254096] [90298180] [93264420] [90204538]|)""",
('B3781', 'THIORDXi') : """(Thioredoxin is a small electron-transfer protein which contains a cysteine
disulfide/dithiol active site. The protein functions in a wide variety of cellular
processes. Thioredoxin is reduced by NADPH in a reaction catalyzed by
thioredoxin reductase. The conversion between the oxidized and reduced
forms results in a change of conformation. The functional properties differ
between the two forms of thioredoxin. The reduced thioredoxin is a powerful
protein disulfide reductase, thioredoxin catalyzes dithiol-disulfide exchange
reactions. The oxidized form of thioredoxin has been crystallized, the reduced
form has been solved by NMR.
|CITS: [85277988] [90198521] [90254096] [90298180] [93264420] [90204538]|)""",
('B2582', 'THIORDXi') : """(The trxC gene encodes a second thioredoxin in E. coli. Thioredoxin 2 can perform many of
thioredoxin 1's roles in vivo; it is able to reduce some essential cytoplasmic enzymes.
Along with thioredoxin 1 and glutaredoxin 1, thioredoxin 2 is one of E. coli's most
effective cytoplasmic disulfide-reducing proteins. Any one of these three is sufficient
to support aerobic growth. |CITS: [98429478] [98049550]|)""",
('B2582', 'THIORDXi') : """NIL""",
('B1440', 'PTRCabcpp') : """(periplasmic binding protein of ABC transporter)""",
('B1440', 'PTRCabcpp') : """(YdcS, YdcT, YdcU and YdcV are uncharacterized
members of the ABC superfamily of transporters
|CITS: [99091701]|. YdcS is the putative
periplasmic binding component, YdcT is the
putative ATP binding component, YdcU and YdcV
are the putative membrane spanning components.
Bases on sequence similarity they may function
together as an ATP-dependent spermidine/
putrecine transporter. The genes ydcS,
ydcT, ydcU, and ydcV are
probably located in a single operon.)""",
('B1441', 'PTRCabcpp') : """(ATP-binding component of ABC transporter)""",
('B1441', 'PTRCabcpp') : """(YdcS, YdcT, YdcU and YdcV are uncharacterized
members of the ABC superfamily of transporters
|CITS: [99091701]|. YdcS is the putative
periplasmic binding component, YdcT is the
putative ATP binding component, YdcU and YdcV
are the putative membrane spanning components.
Bases on sequence similarity they may function
together as an ATP-dependent spermidine/
putrecine transporter. The genes ydcS,
ydcT, ydcU, and ydcV are
probably located in a single operon.)""",
('B1442', 'PTRCabcpp') : """(membrane component of ABC transporter)""",
('B1442', 'PTRCabcpp') : """(YdcS, YdcT, YdcU and YdcV are uncharacterized
members of the ABC superfamily of transporters
|CITS: [99091701]|. YdcS is the putative
periplasmic binding component, YdcT is the
putative ATP binding component, YdcU and YdcV
are the putative membrane spanning components.
Bases on sequence similarity they may function
together as an ATP-dependent spermidine/
putrecine transporter. The genes ydcS,
ydcT, ydcU, and ydcV are
probably located in a single operon.)""",
('B1443', 'PTRCabcpp') : """(membrane component of ABC transporter)""",
('B1443', 'PTRCabcpp') : """(YdcS, YdcT, YdcU and YdcV are uncharacterized
members of the ABC superfamily of transporters
|CITS: [99091701]|. YdcS is the putative
periplasmic binding component, YdcT is the
putative ATP binding component, YdcU and YdcV
are the putative membrane spanning components.
Bases on sequence similarity they may function
together as an ATP-dependent spermidine/
putrecine transporter. The genes ydcS,
ydcT, ydcU, and ydcV are
probably located in a single operon.)""",
('B0684', 'RNTR2c') : """(Flavodoxins are small, acidic electron transfer proteins which contain FMN as a prosthetic group. They are only
able to accept and donate electrons. Flavodoxin is an important member of the multi-enzyme complexes that are
involved in the activation of anaerobic nucleoside reductase and pyruvate-formate lyase. Flavodoxins are
functionally interchangeable with ferredoxins, but some enzymes are specific for one or the other. E. coli has
at least two flavodoxins |CITS: [91154129][95050480][93194782]|.
FldA is essential under both aerobic and anaerobic growth conditions |CITS: [10714981]|. The essential role for
flavodoxin 1 under aerobic conditions is in the MEP pathway for isoprenoid biosynthesis
(|FRAME: NONMEVIPP-PWY|) |CITS: [15978585]|.
Crystal and solution structures of FldA have been solved |CITS: [9416602][9119004]|.)""",
('B0684', 'RNTR2c') : """NIL""",
('B0684', 'RNTR2c') : """(Flavodoxins are small, acidic electron transfer proteins which contain FMN as a prosthetic group. They are only
able to accept and donate electrons. Flavodoxin is an important member of the multi-enzyme complexes that are
involved in the activation of anaerobic nucleoside reductase and pyruvate-formate lyase. Flavodoxins are
functionally interchangeable with ferredoxins, but some enzymes are specific for one or the other. E. coli has
at least two flavodoxins |CITS: [91154129][95050480][93194782]|.
FldA is essential under both aerobic and anaerobic growth conditions |CITS: [10714981]|. The essential role for
flavodoxin 1 under aerobic conditions is in the MEP pathway for isoprenoid biosynthesis
(|FRAME: NONMEVIPP-PWY|) |CITS: [15978585]|.
Crystal and solution structures of FldA have been solved |CITS: [9416602][9119004]|.)""",
('B0684', 'RNTR2c') : """NIL""",
('B2895', 'RNTR2c') : """(Flavodoxins are small, acidic electron transfer proteins
which contain FMN as a prosthetic group. They are only able to accept
and donate electrons. Flavodoxin is an important member of the
multi-enzyme complexes that are involved in the activation of
anaerobic nucleoside reductase and pyruvate-formate lyase. Flavodoxins
are functionally interchangeable with ferredoxins but some enzymes are
specific for one or the other. E. coli has at least two flavodoxins.
|CITS: [91154129] [95050480] [93194782]|)""",
('B2895', 'RNTR2c') : """NIL""",
('B2895', 'RNTR2c') : """(Flavodoxins are small, acidic electron transfer proteins
which contain FMN as a prosthetic group. They are only able to accept
and donate electrons. Flavodoxin is an important member of the
multi-enzyme complexes that are involved in the activation of
anaerobic nucleoside reductase and pyruvate-formate lyase. Flavodoxins
are functionally interchangeable with ferredoxins but some enzymes are
specific for one or the other. E. coli has at least two flavodoxins.
|CITS: [91154129] [95050480] [93194782]|)""",
('B2895', 'RNTR2c') : """NIL""",
('B0433', 'AGM3Pt2pp') : """(AmpG is a member of the major facilitator superfamily of transporters,
and together with AmpD, is essential for induction of the AmpC Β-lactamase
and is involved in the recycling of cell wall peptides
|CITS: [90120556] [94049112] [95291453] [96100441]|.
Mutants in ampG are unable to induce ampC and display greatly
increased cell wall turnover |CITS: [95009971]|.
AmpG is responsible for the transport of precursors of the anhMurNAc tripeptide into the cytoplasm
|CITS:[8878601]|. These precursors are the products of peptidoglycan degradation and include the
disaccharide GlcNAc-anhMurNAc as well as GlcNAc-anhMurNAc-oligopeptides (tri-, tetra-, and
pentapeptides). Transport is dependent on the proton motive force |CITS:[12426329]|.
Following uptake of these muropeptides, they are degraded, releasing the components which can
subsequently be used in cell wall synthesis |CITS: [95302966]|.
Experiments with β-lactamase fusions show AmpG contains two large cytoplasmic loops and 10
transmembrane segments |CITS:[15728916]|.
Cytosolic muramyl peptides probably induce expression of ampC by binding
to its regulator AmpR |CITS: [97302495]|.)""",
('B3469', 'ZN2abcpp') : """(The gene product of the yhhO gene, also referred to as zntA, is
a P-type ATPase involved in the efflux of Pb(II), Cd(II), and Zn(II) |CITS:[98070750] [20263730]|.
ZntA displays a Km of approximately 20 μM for Cd(II) and
100 μM for Zn(II) |CITS:[20127859]|. The transporter appears to be inhibited
by vanadate, a common inhibitor of P-type ATPase. The ATPase activity of the
transporter was found to follow the order Pb(II), Cd(II), Zn(II), and Hg(II) |CITS:[20127859]|.
A zntA mutant showed hypersensitivity to Cd(II) and Zn(II) |CITS:[98070750]|.
The zntA gene was found to be under the control of the transcriptional
regulator ZntR. zntA expression is activated by an increased concentration
of Cd(II) and Zn(II) within the cell, showing greater induction by Cd(II) than by
Zn(II) |CITS:[20127859]|.)""",
('B0572', 'CUt3') : """(CusC is the outer membrane factor for the CusCFBA copper efflux system.
The cusABFCRS gene cluster has similarity to a gene cluster contained on a silver resistance plasmid from a clinical Salmonella isolate |CITS: [12829274]|.
Agr: "Ag(I) resistance" |CITS: [12829274]|.)""",
('B0572', 'CUt3') : """(The Copper transporting efflux system, CusCFBA, is one of at least three systems involved in copper resistance.
CusB is a member of the membrane fusion protein (MFP) family. CusC is the outer membrane factor which forms a channel in the outer membrane.
CusA is the resistance-nodulation-division (RND) permease. CusF is the periplasmic copper binding protein.
The CusCFBA complex may translocate copper from the cytoplasm to the extracellular enviornment across both the inner and outer membrane. Alternatively, the Cus complex
may capture copper in the periplasm and export it outside. Evidence that supports the alternative claim includes the
periplasmic localization of the copper binding protein, CusF, and the assumption that copper access to the RND protein, CusA, may be possible from the cytoplasm as well as the periplasm. |CITS: [12374972]|
)""",
('B0573', 'CUt3') : """(CusF is a periplasmic copper-binding protein that interacts with the CusCBA copper efflux complex. |CITS: [12813074]|
CusF is a pink copper-binding protein. The UV-vis spectrum of copper-containing CusF showed a absorption maximum
around 510 nm, which has not been reported for any other copper proteins. It is believed that CusF may contain a novel
type of copper binding site. |CITS: [12813074]|
The cusABFCRS gene cluster has similarity to a gene cluster contained on a silver resistance plasmid from a clinical Salmonella isolate |CITS: [12829274]|.
Agr: "Ag(I) resistance" |CITS: [12829274]|.)""",
('B0573', 'CUt3') : """(The Copper transporting efflux system, CusCFBA, is one of at least three systems involved in copper resistance.
CusB is a member of the membrane fusion protein (MFP) family. CusC is the outer membrane factor which forms a channel in the outer membrane.
CusA is the resistance-nodulation-division (RND) permease. CusF is the periplasmic copper binding protein.
The CusCFBA complex may translocate copper from the cytoplasm to the extracellular enviornment across both the inner and outer membrane. Alternatively, the Cus complex
may capture copper in the periplasm and export it outside. Evidence that supports the alternative claim includes the
periplasmic localization of the copper binding protein, CusF, and the assumption that copper access to the RND protein, CusA, may be possible from the cytoplasm as well as the periplasm. |CITS: [12374972]|
)""",
('B0574', 'CUt3') : """(CusB is the membrane fusion protein in the CusCFBA copper efflux system. The function of a membrane fusion protein
like CusB may be to bring the outer membrane factor, CusC, closer to the resistance-nodulation-division permease, CusA.
The cusABFCRS gene cluster has similarity to a gene cluster contained on a silver resistance plasmid from a clinical Salmonella isolate |CITS: [12829274]|.
Agr: "Ag(I) resistance" |CITS: [12829274]|.)""",
('B0574', 'CUt3') : """(The Copper transporting efflux system, CusCFBA, is one of at least three systems involved in copper resistance.
CusB is a member of the membrane fusion protein (MFP) family. CusC is the outer membrane factor which forms a channel in the outer membrane.
CusA is the resistance-nodulation-division (RND) permease. CusF is the periplasmic copper binding protein.
The CusCFBA complex may translocate copper from the cytoplasm to the extracellular enviornment across both the inner and outer membrane. Alternatively, the Cus complex
may capture copper in the periplasm and export it outside. Evidence that supports the alternative claim includes the
periplasmic localization of the copper binding protein, CusF, and the assumption that copper access to the RND protein, CusA, may be possible from the cytoplasm as well as the periplasm. |CITS: [12374972]|
)""",
('B1440', 'SPMDabcpp') : """(periplasmic binding protein of ABC transporter)""",
('B1440', 'SPMDabcpp') : """(YdcS, YdcT, YdcU and YdcV are uncharacterized
members of the ABC superfamily of transporters
|CITS: [99091701]|. YdcS is the putative
periplasmic binding component, YdcT is the
putative ATP binding component, YdcU and YdcV
are the putative membrane spanning components.
Bases on sequence similarity they may function
together as an ATP-dependent spermidine/
putrecine transporter. The genes ydcS,
ydcT, ydcU, and ydcV are
probably located in a single operon.)""",
('B1441', 'SPMDabcpp') : """(ATP-binding component of ABC transporter)""",
('B1441', 'SPMDabcpp') : """(YdcS, YdcT, YdcU and YdcV are uncharacterized
members of the ABC superfamily of transporters
|CITS: [99091701]|. YdcS is the putative
periplasmic binding component, YdcT is the
putative ATP binding component, YdcU and YdcV
are the putative membrane spanning components.
Bases on sequence similarity they may function
together as an ATP-dependent spermidine/
putrecine transporter. The genes ydcS,
ydcT, ydcU, and ydcV are
probably located in a single operon.)""",
('B1442', 'SPMDabcpp') : """(membrane component of ABC transporter)""",
('B1442', 'SPMDabcpp') : """(YdcS, YdcT, YdcU and YdcV are uncharacterized
members of the ABC superfamily of transporters
|CITS: [99091701]|. YdcS is the putative
periplasmic binding component, YdcT is the
putative ATP binding component, YdcU and YdcV
are the putative membrane spanning components.
Bases on sequence similarity they may function
together as an ATP-dependent spermidine/
putrecine transporter. The genes ydcS,
ydcT, ydcU, and ydcV are
probably located in a single operon.)""",
('B1443', 'SPMDabcpp') : """(membrane component of ABC transporter)""",
('B1443', 'SPMDabcpp') : """(YdcS, YdcT, YdcU and YdcV are uncharacterized
members of the ABC superfamily of transporters
|CITS: [99091701]|. YdcS is the putative
periplasmic binding component, YdcT is the
putative ATP binding component, YdcU and YdcV
are the putative membrane spanning components.
Bases on sequence similarity they may function
together as an ATP-dependent spermidine/
putrecine transporter. The genes ydcS,
ydcT, ydcU, and ydcV are
probably located in a single operon.)""",
('B0839', 'MDDCP5pp') : """(DacC is a penicillin-binding protein that is required for proper cell morphology and provides
some resistance to penicillin |CITS: [1447130][12354237][6215397]|. It is one of four DD-carboxypeptidase
low-molecular weight PBPs in Escherichia coli (along with PBP4, PBP6 and DacD) that modify
peptidoglycans through the removal of the terminal D-alanine from pentapeptide side chains |CITS:[368033]|,
|CITS:[8955390]|.
The carboxy-terminus of DacC is capable of forming an alpha helix and interacts with
membranes chiefly through hydrophobic forces |CITS: [9371419][9858668]|.
Deletion of this membrane-anchoring portion of the protein produces soluble DacC. Whereas
overexpression of native DacC results in membrane vesicles in the cystoplasm, overexpression
of this soluble variant yields inclusion bodies. Both forms of DacC can be purified with
Procion rubine MX-B and subsequently bind stoichiometrically with penicillin |CITS: [1447130]|.
Despite being part of a family of D-alanine carboxypeptidases, DacC lacks detectable activity
against bisacetyl-L-lysine-D-alanyl-D-alanine and other test substrates |CITS: [1447130]|.
Deletions in dacC are viable, though slightly penicillin sensitive |CITS: [6215397]|.
dacC dacA double mutants are viable, though they show defects in morphology and cell division
when bolA, which is required for dacC expression on entry to stationary phase, is overexpressed |CITS: [3903044][12354237][2684651]|.
A complete deletion of dacA-D is also viable, as is a strain lacking eight of the known penicillin-binding protein genes,
dacC among them |CITS: [8955390][10383966]|. Overexpression of DacC allows cell division in ftsI23 mutants, but leads to cell
lysis during early exponential growth |CITS: [2254246][11325933]|.)""",
('B2519', 'MPTG2') : """(The PbpC protein contains both a penicillin-binding and a transglycosylase domain. Deletion of the pbpC gene
does not cause an obvious phenotype, and overproduction of the PbpC protein does not rescue the defect of a
ponAts ponB double mutant |CITS: [10542235]|.
PbpC interacts with PBP1B, PBP3, and MltA |CITS: [10542235]|.)""",
('B3396', 'MPTG2') : """(PBP1A is the product of the mrcA gene |CITS:[3882429]|. PBP1A is a bifunctional, inner membrane enzyme
catalyzing the transglycosylation and transpeptidation of murein (peptidoglycan) precursors in the formation of the
murein sacculus |CITS:[9529891]|. The amino terminus contains a signal sequence |CITS:[3882429]|. PBP1A is able
to dimerize without disulfide bonds, but doesn't form a complex with PBP1B |CITS:[12057973]|. Either PBP1A or
PBP1B (the other major bifunctional enzyme in murein synthesis with a different penicillin-binding affinity) is required
for cell elongation because a PBP1A-PBP1B double mutation is lethal |CITS:[1103132][341159][345275][2993822]|.
Experiments have been performed involving inhibition or mutation of PBP1A alone or coupled with inhibition or
mutation of other proteins involved in cell division and murein metabolism |CITS:[7007327][2211517][2066344][10383966]|.)""",
('B3792', 'ECAtpp') : """(WzxE is a "flippase" responsible for movement of lipid III
(Fuc4NAc-ManNAcA-GlcNAc-P-P-undecaprenol)
across the membrane bilayer |CITS: [12621029]|.
The determinants of WzxE recognition of its substrate
have been examined |CITS: [12621029]|.
A wzxE mutant exhibits buildup of lipid III |CITS: [12621029]|.
A wzxE mutant also exhibits a defect in transport of an
N-acetylglucosaminylpyrophosphorylnerol substrate across
membranes in an in vitro system |CITS: [12621029]|.)""",
('B3792', 'ECAtpp') : """(The Enterobacterial Common Antigen biosynthesis protein complex is responsible for synthesizing ECA
polysaccharide chains from Lipid III precursors that have been transferred accross the inner membrane.)""",
('B0411', 'URItex') : """(Tsx is a protein involved with the permeation of ribo- and deoxy-nucleosides, across the outer membrane of E. coli.
It also allows the entry of the antibiotic albicidin, and serves as a receptor for bacteriophage and colicins |CITS: [3276691]|
It is believed to form a 14 strand β-barrel porin.
The crystal structure of Tsx has been determined up to 3.1 A co-crystallized with a range of nucleosides |CITS:[15272310]|. Tsx has been shown to localize to the cellular poles |CITS:[15130122]|.)""",
('B1329', '3PEPTabcpp') : """(Periplasmic binding component of Murein Tripeptide ABC Transporter |CITS:[9495761]|.)""",
('B1329', '3PEPTabcpp') : """(OppABCDF is an ATP-dependent oligopeptide transporter that is a
member of the ATP-Binding Cassette (ABC) Superfamily of transporters |CITS:[1738314]|.
OppABCDF has not been investigated in detail in E. coli,
but the orthologous system in Salmonella typhimurium has been
extensively characterized. Binding affinity and competition assays have
shown that OppABCDF will transport oligopeptides up to five amino acids
in length, but has no affinity for free amino acids |CITS:[3536860],[8801122]|.
The system has been observed to function in oligopeptide uptake, as
well as recycling of cell wall peptides |CITS:[2821267]|. Based on
sequence similarity, OppB and OppC are the membrane components
of the ABC transporter, and OppD and OppF are the ATP-binding
components of the ABC transporter |CITS:[8801122],[1738314]|.
OppA is the periplasmic substrate-binding component, however MppA
can replace OppA as a periplasmic-binding component of the transporter
when it binds murein tripeptides |CITS:[9495761]|. MppA was shown to be
required for murein tripeptide transport in a diaminoimelic acid-requiring
strain |CITS:[9495761]|. Insertion mutation of the oppF gene has
shown that OppF is required for Opp transporter function |CITS:[2821267]|.
In addition, Insertional mutants of each of the opp genes were
constructed, and the opp-minus strains were unable to utilize the
peptide Pro-Gly-Gly, normally transported by the wild-type transporter |CITS:[2821267]|.
Expression of oppABCD increased after long-term adaptation
to growth in complex medium with acetate or propionate |CITS:[12620868]|.
Expression of mppA decreased after long-term adaptation to growth
in complex medium with acetate or propionate |CITS:[12620868]|.
Expression of mppA was shown to be activated by cyclic AMP
receptor protein |CITS:[15520470]|.
)""",
('B2458', 'PTAr') : """(No information about this protein was found by a literature search conducted on January 20, 2006.)""",
('B0433', 'AGMt2pp') : """(AmpG is a member of the major facilitator superfamily of transporters,
and together with AmpD, is essential for induction of the AmpC Β-lactamase
and is involved in the recycling of cell wall peptides
|CITS: [90120556] [94049112] [95291453] [96100441]|.
Mutants in ampG are unable to induce ampC and display greatly
increased cell wall turnover |CITS: [95009971]|.
AmpG is responsible for the transport of precursors of the anhMurNAc tripeptide into the cytoplasm
|CITS:[8878601]|. These precursors are the products of peptidoglycan degradation and include the
disaccharide GlcNAc-anhMurNAc as well as GlcNAc-anhMurNAc-oligopeptides (tri-, tetra-, and
pentapeptides). Transport is dependent on the proton motive force |CITS:[12426329]|.
Following uptake of these muropeptides, they are degraded, releasing the components which can
subsequently be used in cell wall synthesis |CITS: [95302966]|.
Experiments with β-lactamase fusions show AmpG contains two large cytoplasmic loops and 10
transmembrane segments |CITS:[15728916]|.
Cytosolic muramyl peptides probably induce expression of ampC by binding
to its regulator AmpR |CITS: [97302495]|.)""",
('B0839', 'MDDCP4pp') : """(DacC is a penicillin-binding protein that is required for proper cell morphology and provides
some resistance to penicillin |CITS: [1447130][12354237][6215397]|. It is one of four DD-carboxypeptidase
low-molecular weight PBPs in Escherichia coli (along with PBP4, PBP6 and DacD) that modify
peptidoglycans through the removal of the terminal D-alanine from pentapeptide side chains |CITS:[368033]|,
|CITS:[8955390]|.
The carboxy-terminus of DacC is capable of forming an alpha helix and interacts with
membranes chiefly through hydrophobic forces |CITS: [9371419][9858668]|.
Deletion of this membrane-anchoring portion of the protein produces soluble DacC. Whereas
overexpression of native DacC results in membrane vesicles in the cystoplasm, overexpression
of this soluble variant yields inclusion bodies. Both forms of DacC can be purified with
Procion rubine MX-B and subsequently bind stoichiometrically with penicillin |CITS: [1447130]|.
Despite being part of a family of D-alanine carboxypeptidases, DacC lacks detectable activity
against bisacetyl-L-lysine-D-alanyl-D-alanine and other test substrates |CITS: [1447130]|.
Deletions in dacC are viable, though slightly penicillin sensitive |CITS: [6215397]|.
dacC dacA double mutants are viable, though they show defects in morphology and cell division
when bolA, which is required for dacC expression on entry to stationary phase, is overexpressed |CITS: [3903044][12354237][2684651]|.
A complete deletion of dacA-D is also viable, as is a strain lacking eight of the known penicillin-binding protein genes,
dacC among them |CITS: [8955390][10383966]|. Overexpression of DacC allows cell division in ftsI23 mutants, but leads to cell
lysis during early exponential growth |CITS: [2254246][11325933]|.)""",
('B2690', 'PGMT') : """(Phosphatase activity of YqaB was discovered in a high-throughput screen of purified proteins |CITS: [15808744]|.
)""",
('B0411', 'ADNtex') : """(Tsx is a protein involved with the permeation of ribo- and deoxy-nucleosides, across the outer membrane of E. coli.
It also allows the entry of the antibiotic albicidin, and serves as a receptor for bacteriophage and colicins |CITS: [3276691]|
It is believed to form a 14 strand β-barrel porin.
The crystal structure of Tsx has been determined up to 3.1 A co-crystallized with a range of nucleosides |CITS:[15272310]|. Tsx has been shown to localize to the cellular poles |CITS:[15130122]|.)""",
('B2582', 'METSOXR2') : """(The trxC gene encodes a second thioredoxin in E. coli. Thioredoxin 2 can perform many of
thioredoxin 1's roles in vivo; it is able to reduce some essential cytoplasmic enzymes.
Along with thioredoxin 1 and glutaredoxin 1, thioredoxin 2 is one of E. coli's most
effective cytoplasmic disulfide-reducing proteins. Any one of these three is sufficient
to support aerobic growth. |CITS: [98429478] [98049550]|)""",
('B2582', 'METSOXR2') : """NIL""",
('B3781', 'METSOXR2') : """(Thioredoxin is a small electron-transfer protein which contains a cysteine
disulfide/dithiol active site. The protein functions in a wide variety of cellular
processes. Thioredoxin is reduced by NADPH in a reaction catalyzed by
thioredoxin reductase. The conversion between the oxidized and reduced
forms results in a change of conformation. The functional properties differ
between the two forms of thioredoxin. The reduced thioredoxin is a powerful
protein disulfide reductase, thioredoxin catalyzes dithiol-disulfide exchange
reactions. The oxidized form of thioredoxin has been crystallized,
the reduced form has been solved by NMR. |CITS: [85277988] [90198521]
[90254096] [90298180] [93264420] [90204538]|)""",
('B3781', 'METSOXR2') : """(Thioredoxin is a small electron-transfer protein which contains a cysteine
disulfide/dithiol active site. The protein functions in a wide variety of cellular
processes. Thioredoxin is reduced by NADPH in a reaction catalyzed by
thioredoxin reductase. The conversion between the oxidized and reduced
forms results in a change of conformation. The functional properties differ
between the two forms of thioredoxin. The reduced thioredoxin is a powerful
protein disulfide reductase, thioredoxin catalyzes dithiol-disulfide exchange
reactions. The oxidized form of thioredoxin has been crystallized, the reduced
form has been solved by NMR.
|CITS: [85277988] [90198521] [90254096] [90298180] [93264420] [90204538]|)""",
('B1605', 'ARGORNt7pp') : """(ArcD is an uncharacterised member of the APC family of
amino acid transporters. ArcD is highly similar to the
Pseudomonas aeruginosa ArcD arginine/ornithine
antiporter and probably has a similar function.)""",
('B2582', 'METSOXR1') : """(The trxC gene encodes a second thioredoxin in E. coli. Thioredoxin 2 can perform many of
thioredoxin 1's roles in vivo; it is able to reduce some essential cytoplasmic enzymes.
Along with thioredoxin 1 and glutaredoxin 1, thioredoxin 2 is one of E. coli's most
effective cytoplasmic disulfide-reducing proteins. Any one of these three is sufficient
to support aerobic growth. |CITS: [98429478] [98049550]|)""",
('B2582', 'METSOXR1') : """NIL""",
('B3781', 'METSOXR1') : """(Thioredoxin is a small electron-transfer protein which contains a cysteine
disulfide/dithiol active site. The protein functions in a wide variety of cellular
processes. Thioredoxin is reduced by NADPH in a reaction catalyzed by
thioredoxin reductase. The conversion between the oxidized and reduced
forms results in a change of conformation. The functional properties differ
between the two forms of thioredoxin. The reduced thioredoxin is a powerful
protein disulfide reductase, thioredoxin catalyzes dithiol-disulfide exchange
reactions. The oxidized form of thioredoxin has been crystallized,
the reduced form has been solved by NMR. |CITS: [85277988] [90198521]
[90254096] [90298180] [93264420] [90204538]|)""",
('B3781', 'METSOXR1') : """(Thioredoxin is a small electron-transfer protein which contains a cysteine
disulfide/dithiol active site. The protein functions in a wide variety of cellular
processes. Thioredoxin is reduced by NADPH in a reaction catalyzed by
thioredoxin reductase. The conversion between the oxidized and reduced
forms results in a change of conformation. The functional properties differ
between the two forms of thioredoxin. The reduced thioredoxin is a powerful
protein disulfide reductase, thioredoxin catalyzes dithiol-disulfide exchange
reactions. The oxidized form of thioredoxin has been crystallized, the reduced
form has been solved by NMR.
|CITS: [85277988] [90198521] [90254096] [90298180] [93264420] [90204538]|)""",
('B0849', 'RNDR4b') : """NIL""",
('B0849', 'RNDR4b') : """(Glutaredoxins are ubiquitous proteins that catalyze the reduction of disulfides via reduced glutathione (GSH).
Escherichia coli has three glutaredoxins (Grx1, Grx2, and Grx3) containing the classic dithiol active site
CPYC, and a fourth one which contains a monothiol (CGFS) potential active site |CITS: [15833738]|.
The glutaredoxins act as a cofactor enabling intracellular redox reactions through a disulfide/dithiol
enzymatic mechanism involving the active site cysteines. They are used as a
hydrogen donor for the glutathione(GSH)-dependent synthesis of deoxyribonucleotides
by ribonucleotide reductase and reduces specific cysteine residues in
ribonucleotide reductase.
Glutaredoxin are also a hydrogen donor for the reduction of adenosine 3'-phosphate 5'-phosphosulfate
and methionine sulfoxide.
In addition, glutaredoxins also catalyzes GSH-disulfide oxidoreduction reactions with low molecular weight
substrates. |CITS: [79151138] [91242463] [93003075]| There are two additional
glutaredoxins in E. coli whose physiological roles have not been fully
determined. |CITS: [95024051]|)""",
('B1064', 'RNDR4b') : """(Glutaredoxins are ubiquitous proteins that catalyze the reduction of disulfides via reduced glutathione (GSH).
Escherichia coli has three glutaredoxins (Grx1, Grx2, and Grx3) containing the classic dithiol active site
CPYC, and a fourth one which contains a monothiol (CGFS) potential active site |CITS: [15833738]|.
The glutaredoxins do not act as enzymes, but rather as a cofactor, enabling intracellular redox reactions through
a disulfide/dithiol enzymatic mechanism involving the active site cysteines.
There is almost no similarity between the amino acid sequence of Grx2 (an approximately 27 kDa protein) and Grx1
or Grx3 (both 9-kDa proteins), with the exception of the active site which is identical in all three glutaredoxins.
In contrast to glutaredoxin 1 and 3, Grx 2 is not a hydrogen donor for ribonucleotide reductase.
On the other hand, Grx2 is the primary hydrogen donor to ArsC-catalyzed arsenate reduction (|FRAME: RXN-982|)
|CITS: [10593884]|. It is also the most abundant glutaredoxin in the cell, with an intracellular concentration
of 5 µM, compared with 0.2 µM and 2.4 µM for Grx1 and 3, respectively |CITS: [10593884]|.)""",
('B1064', 'RNDR4b') : """(Glutaredoxins are ubiquitous proteins that catalyze the reduction of disulfides via reduced glutathione (GSH).
Escherichia coli has three glutaredoxins (Grx1, Grx2, and Grx3) containing the classic dithiol active site
CPYC, and a fourth one which contains a monothiol (CGFS) potential active site |CITS: [15833738]|.
The glutaredoxins do not act as enzymes, but rather as a cofactor, enabling intracellular redox reactions through
a disulfide/dithiol enzymatic mechanism involving the active site cysteines.
There is almost no similarity between the amino acid sequence of Grx2 (an approximately 27 kDa protein) and Grx1
or Grx3 (both 9-kDa proteins), with the exception of the active site which is identical in all three glutaredoxins.
In contrast to glutaredoxin 1 and 3, Grx 2 is not a hydrogen donor for ribonucleotide reductase.
On the other hand, Grx2 is the primary hydrogen donor to ArsC-catalyzed arsenate reduction (|FRAME: RXN-982|)
|CITS: [10593884]|. It is also the most abundant glutaredoxin in the cell, with an intracellular concentration
of 5 µM, compared with 0.2 µM and 2.4 µM for Grx1 and 3, respectively |CITS: [10593884]|.)""",
('B3610', 'RNDR4b') : """(There at least three glutaredoxins in E. coli. Glutaredoxin
3 is able to function as a disulfide reductase, but not as well as
glutaredoxin 1. Coupled with cellular glutathione it may be the third
hydrogen donor system in the absence of thioredoxin and glutaredoxin
1. Under normal conditions it is likely that glutaredoxin has other
functions. |CITS: [95024051] [96215095]|)""",
('B3610', 'RNDR4b') : """NIL""",
('B1654', 'RNDR4b') : """(Grx4 belongs to the family of monothiol glutaredoxins. Oxidized Grx4 can be reduced by the thioredoxin system or
glutaredoxin 1. Grx4 is not active in the standard glutaredoxin assay |CITS: [15833738]|.
Grx4 is an abundant protein that is upregulated during stationary phase; the increased expression is dependent on
ppGpp |CITS: [15833738]|.
A grxD null mutant could not be obtained |CITS: [15833738]|. grxD has previously been reported to be
essential for aerobic growth in rich media |CITS: [13129938]|.
A solution structure of the reduced form of Grx4 has been determined |CITS: [15840565]|)""",
('B0657', 'ALPATE160pp') : """(Apolipoprotein N-acyltransferase activity transfers palmitate to apolipoproteins, resulting in the maturation of lipoproteins from apolipoprotein precursors |CITS: [2032623]|. Aminoacylation of lipoproteins bound for the outer membrane is required for proper localization of these lipoproteins via the Lol pathway |CITS: [12198129]|.
The enzyme activity has been characterized |CITS: [2032623]|. The enzyme can utilize the phospholipids phosphatidylethanolamine, phosphatidylglycerol, or cardiolipin in vitro |CITS: [2032623]|. A pss mutant exhibits apolipoprotein N-acyltransferase activity, indicating that the enzyme is not specific for a phosphatidylethanolamine donor in vivo |CITS: [2033085]|.
Apolipoprotein N-acyltransferase localizes to inner membrane or inner-plus-outer membrane fractions |CITS: [2032623]|.
A cutE mutant exhibits copper sensitivity |CITS: [1938881]|.
CutE has a region with similarity to copper binding sites |CITS: [1938881]|.
CutE functionally complements the heat sensitivity, copper sensitivity, and apolipoprotein N-acyltransferase defect of a Salmonella typhimurium SE5312 mutant |CITS: [8344936]|. CutE overproduction in Salmonella typhimurium results in increased apolipoprotein N-acyltransferase activity |CITS: [8344936]|.
CutE has similarity to Rhizobium meliloti ActA |CITS: [8868435]|.
Regulation has been described |CITS: [1938881]|.
Review: |CITS: [7651187]|.)""",
('B1677', 'ALPATE160pp') : """(Lpp, the major lipoprotein, is one of the most abundant proteins in Escherichia coli |CITS:[4610570]| and is
necessary for the stabilization and integrity of the bacterial cell envelope |CITS:[11790745]|. The three-dimensional crystal structure of Lpp has been determined to 1.9 A resolution |CITS:[10843861]|. Cells lacking Lpp or with mutations affecting the attachment of Lpp to the murein (peptidoglycan) layer exhibit outer membrane blebs, are hypersensitive to toxic compounds, and release periplasmic proteins to the extracellular medium |CITS:[105245]|. Lpp exists in two forms, a free form and a covalently linked bound form attached to the peptidoglycan. Both forms are localized to the outer membrane |CITS:[4245367]|, |CITS:[4565677]|. Lpp is expressed as a prolipoprotein, having 20 amino acid residues extending from the amino terminus |CITS:[322142]| During translocation across the cytoplasmic membrane, the prolipoprotein undergoes modifications of the amino terminus cysteine residue followed by cleavage of the signal peptide extension |CITS:[8051048]|. The mature lipoprotein is then translocated to the outer membrane where it is covalently bound to the peptidoglycan layer |CITS:[6369111]|, |CITS:[6363408]|. Globomycin was found to inhibit the cleavage by signal peptidase II through noncompetitive binding to the enzyme |CITS:[3888977]|. Studies using inhibitors of the proton motive force (pmf) and ATP-depleted cells indicated that both the pmf and ATP are required for translocation of an OmpF-Lpp chimeric protein |CITS:[3029075]|. Translocation across the inner membrane was found to involve the Sec export apparatus |CITS:[2842297]|. Immunoelectron microscopy revealed that free lipoprotein is inserted equally over the entire cell wall, that lipoprotein synthesis increases with cell length, and that cell shape depends on total lipoprotein content of the cell in that low total lipoprotein corresponds to a spherical shape and a higher lipoprotein content corresponds with a rod shape |CITS:[3316185]|. Pulse-chase labeling followed by cell fractionation found that Lpp utilizes the LolA-LolB system to facilitate its release from the inner membrane and localization to the outer membrane |CITS:[10521496]|. Chemical cross-linking has revealed that Lpp organizes into trimers and interacts with OmpA, a major outer membrane lipoprotein |CITS:[3013869]|.)""",
('B3577', 'XYLUt2pp') : """(Based on sequence similarity, YiaM is a membrane-spanning component of the YiaMNO Binding Protein-dependent Secondary (TRAP) Transporter |CITS:[11524131]|)""",
('B3577', 'XYLUt2pp') : """(Based on sequence similarity, the yiaMNO genes encode the only tri-partite
ATP-independent periplasmic (TRAP) transporter in Escherichia coli. The TRAP
transporters share characteristics of both the ATP-binding cassette (ABC) and secondary
families of transporters |CITS:[11524131]|. Like the ABC transporters TRAP
transporters use an extracytoplasmic solute-binding protein but rather than ATP hydrolysis
the driving force is provided by either proton-(pmf) and/or sodium ion motive
force (smf) |CITS:[11524131]|. Based on sequence similarity, YiaO is the periplasmic
solute-binding protein and YiaM and YiaN are membrane-spanning proteins.
Deletion mutation experiments |CITS:[14668138]| showed that deletion of the yiaMNO
genes affected the ability of E.coli to utilize L-xylulose when
growth was measured using various carbon substrates. Solute transport studies
|CITS:[14668138]| determined that the yiaMNO deletion strain was capable
of utilizing L-xylulose but at a lower rate, indicating that the YiaMNO transporter is
involved in, but not essential for L-xylulose utilization. Purification and binding
studies |CITS:[14668138]| using YiaO showed that YiaO was able to bind L-xylulose.
Furthermore, spheroblasts expressing the YiaMN membrane domains were
stimulated to increase uptake of L-xylulose when incubated with the periplasmic
substrate-binding YiaO while those spheroblasts not expressing YiaMN showed no
such stimulation. Deletion of yiaMNO resulted in a delay of entry into stationary phase of cells
grown in LB with glucose, or minimal medium with glucose or other compounds. These cultures obtained a
higher stationary phase OD660 and higher c.f.u. numbers. Deletion of yiaMNO also
resulted in an increased lag time in cultures with high NaCl concentrations, and a reduction in biofilm
formation in minimal medium with glucose |CITS:[15870475]|.)""",
('B3578', 'XYLUt2pp') : """(Based on sequence similarity, YiaN is a membrane-spanning component of the YiaMNO Binding protein-dependent Secondary (TRAP) Transporter |CITS:[11524131]|.)""",
('B3578', 'XYLUt2pp') : """(Based on sequence similarity, the yiaMNO genes encode the only tri-partite
ATP-independent periplasmic (TRAP) transporter in Escherichia coli. The TRAP
transporters share characteristics of both the ATP-binding cassette (ABC) and secondary
families of transporters |CITS:[11524131]|. Like the ABC transporters TRAP
transporters use an extracytoplasmic solute-binding protein but rather than ATP hydrolysis
the driving force is provided by either proton-(pmf) and/or sodium ion motive
force (smf) |CITS:[11524131]|. Based on sequence similarity, YiaO is the periplasmic
solute-binding protein and YiaM and YiaN are membrane-spanning proteins.
Deletion mutation experiments |CITS:[14668138]| showed that deletion of the yiaMNO
genes affected the ability of E.coli to utilize L-xylulose when
growth was measured using various carbon substrates. Solute transport studies
|CITS:[14668138]| determined that the yiaMNO deletion strain was capable
of utilizing L-xylulose but at a lower rate, indicating that the YiaMNO transporter is
involved in, but not essential for L-xylulose utilization. Purification and binding
studies |CITS:[14668138]| using YiaO showed that YiaO was able to bind L-xylulose.
Furthermore, spheroblasts expressing the YiaMN membrane domains were
stimulated to increase uptake of L-xylulose when incubated with the periplasmic
substrate-binding YiaO while those spheroblasts not expressing YiaMN showed no
such stimulation. Deletion of yiaMNO resulted in a delay of entry into stationary phase of cells
grown in LB with glucose, or minimal medium with glucose or other compounds. These cultures obtained a
higher stationary phase OD660 and higher c.f.u. numbers. Deletion of yiaMNO also
resulted in an increased lag time in cultures with high NaCl concentrations, and a reduction in biofilm
formation in minimal medium with glucose |CITS:[15870475]|.)""",
('B3579', 'XYLUt2pp') : """(Based on sequence similarity, YiaO is the periplasmic solute-binding component of the YiaMNO Binding Protein-dependent Secondary (TRAP) transporter)""",
('B3579', 'XYLUt2pp') : """(Based on sequence similarity, the yiaMNO genes encode the only tri-partite
ATP-independent periplasmic (TRAP) transporter in Escherichia coli. The TRAP
transporters share characteristics of both the ATP-binding cassette (ABC) and secondary
families of transporters |CITS:[11524131]|. Like the ABC transporters TRAP
transporters use an extracytoplasmic solute-binding protein but rather than ATP hydrolysis
the driving force is provided by either proton-(pmf) and/or sodium ion motive
force (smf) |CITS:[11524131]|. Based on sequence similarity, YiaO is the periplasmic
solute-binding protein and YiaM and YiaN are membrane-spanning proteins.
Deletion mutation experiments |CITS:[14668138]| showed that deletion of the yiaMNO
genes affected the ability of E.coli to utilize L-xylulose when
growth was measured using various carbon substrates. Solute transport studies
|CITS:[14668138]| determined that the yiaMNO deletion strain was capable
of utilizing L-xylulose but at a lower rate, indicating that the YiaMNO transporter is
involved in, but not essential for L-xylulose utilization. Purification and binding
studies |CITS:[14668138]| using YiaO showed that YiaO was able to bind L-xylulose.
Furthermore, spheroblasts expressing the YiaMN membrane domains were
stimulated to increase uptake of L-xylulose when incubated with the periplasmic
substrate-binding YiaO while those spheroblasts not expressing YiaMN showed no
such stimulation. Deletion of yiaMNO resulted in a delay of entry into stationary phase of cells
grown in LB with glucose, or minimal medium with glucose or other compounds. These cultures obtained a
higher stationary phase OD660 and higher c.f.u. numbers. Deletion of yiaMNO also
resulted in an increased lag time in cultures with high NaCl concentrations, and a reduction in biofilm
formation in minimal medium with glucose |CITS:[15870475]|.)""",
('B2835', '2AGPA180tipp') : """(LplT is a major facilitator superfamily (MFS) protein that acts as a flippase for transbilayer movement of
lysophospholipids. Mutation experiments and
transporter assays have determined LplT is responsible for the facilitated diffusion of lysophospholipids to
the cytoplasmic portion of the inner membrane providing substrate for the bifunctional enzyme
2-acyl-GPE acyltransferase/acyl-ACP synthetase (Aas). lplT forms an operon with the aas
gene |CITS:[15661733]|.)""",
('B2701', 'MLTGY4pp') : """(MltB is one of three (along with MltA and Slt70) major lytic endotransglycosylases expressed in
Escherichia coli. MltA and MltB are expressed as membrane-bound lipoproteins. Expression
of MltB in cells grown in the presence of H-3 palmitate followed by SDS-PAGE analysis resulted in
fluorographic visualization of a labeled band corresponding to the 36 kDa mass of MltB, demonstrating
the lipoprotein character of MltB. Additionally, in the presence of globomycin, an inhibitor of the
lipoprotein signal peptidase, a larger protein, the prolipoprotein form of MltB, was found to accumulate.
Overexpression of mltB resulted in a 55-fold increase in murein hydrolase activity in the membrane
fraction and subsequent cell lysis. Membrane fractionation followed by sucrose-density-gradient
centrifugation indicated that most of the induced hydrolytic activity was located in the outer and
intermediate membrane fractions. A deletion of the mltB gene showed no obvious phenotype
|CITS:[746170]|, while a triple mltA, mltB, and slt70 mutant resulted in a 72%
reduction in murein turnover |CITS:[10572120]|.)""",
('B1193', 'MLTGY4pp') : """(EmtA is a lytic endotransglycosylase which is expressed in Escherichia coli as a membrane-bound lipoprotein.
Overexpression of emtA results in the hydrolysis of glycan strands isolated from the murein (peptidoglycan)
sacculus, which serves as a bacterial exoskeleton |CITS:[9642199]|. It is believed that the emtA gene product,
like other murein hydrolases, is involved in cleavage of the net-like murein structure thereby allowing for cell enlargement
and division and also for localized opening of the peptidoglycan layer to allow the export of bulky compounds such as DNA,
toxins, flagella, and fimbrial proteins |CITS:[8824596]|, |CITS:[9642199]|.)""",
('B2963', 'MLTGY4pp') : """(E. coli contains a large number of murein hydrolase enzymes. MltC belongs to the family of lytic
transglycosylases which degrade GlcNAcMurNAc glycan strands, resulting in the formation of a
1,6-anhydro-MurNAc residue at the released product. These enzymes are involved in the cleavage of the septum
during cell division.
Peptidoglycan hydrolase activity of MltC was demonstrated |CITS: [9158737]|.
A mutant containing deletions in mltC, mltD, and mltE has a defect in cell separation, growing as
short chains of cells |CITS: [12399477]|. These chain-forming mutants have a defect in the barrier function of the
outer membrane. A mutant strain lacking all six known lytic transglycosylases (mltA mltB mltC mltD mltE slt) is
unable to induce β-lactamase and is more susceptible to certain high-molecular weight antibiotics which are
normally inactive against Gram-negative bacteria, such as bacitracin, gallidermin and vancomycin |CITS: [15793119]|.
Expression of mltC is induced by oxidative stress via SoxS |CITS: [14594836]|.
Review: |CITS: [7487333]|)""",
('B4392', 'MLTGY4pp') : """(Slt70 is involved in growth and recycling of peptidoglycan by catalyzing
the lysis of the β-1,4 glycosidic bond between N-acetylmuramic
acid and N-acetylglucosamine, producing 1,6-anhydromuropeptides at
an optimal pH of 4.5 with a Km of 200 mg/L |CITS:[357]|.
Slt70 forms a murein-metabolizing multi-enzyme complex with PBP3 and
PBP7/8 |CITS:[8063800]|. PBP7/8 was shown to stabilize and stimulate the
activity of Slt70 |CITS:[8063800]|. Slt70 activity is also modulated by the
stringent response |CITS:[1970319]|.
The structure of Slt70 has been determined by X-ray crystallography
revealing a α-superhelix structure with the catalytic domain on
top |CITS:[2184239],[8107871]|. The structure has also been determined
to a resolution of 1.65 Å for its native form, 1.90 Å as a
complex with 1,6-anhydromuropeptide |CITS:[10452894]|, and 2.8 Å
as a complex with bulgecin A |CITS:[7548026]|, its inhibitor |CITS:[1400320]|.
Overproduction of Slt70 resulted in growth inhibition and lysis of some cells,
but a deletion mutant had no observable phenotype |CITS:[1938883]|.
Review: |CITS:[9529891]|
)""",
('B2813', 'MLTGY4pp') : """(MltA is one of three (along with MltB and Slt70) major lytic endotransglycosylases expressed in Escherichia coli.
MltA and MltB are expressed as membrane-bound lipoproteins. Overexpression of MltA resulted in elevated levels of
a membrane fraction protein with a molecular mass corresponding to the mass of the purified MltA protein |CITS:[8288527]|.
Expression of MltA in cells grown in the presence of H-3 palmitate followed by SDS-PAGE analysis resulted in
fluorographic visualization of a labeled band corresponding to the 39 kDa mass of MltA, demonstrating the lipoprotein
character of MltA |CITS:[6988430]|. Sucrose gradient centrifugation studies have shown that MltA is localized to the
outer membrane |CITS:[9287002]|. Induced overexpression of MltA resulted in lysis of cells grown at 30 degrees Celsius,
the optimal temperature for enzymatic activity, but not at 37 degrees. Furthermore the expressed activity was able to
hydrolyze both murein sacculi as well as isolated glycan strands |CITS:[9287002]|. A triple mltA, mltB, and
slt70 mutant resulted in a 72% reduction in murein turnover |CITS:[10572120]|.)""",
('B1094', 'ACOATA') : """(Acyl carrier protein (ACP) plays an important role in fatty
acid biosynthesis. It carries fatty acid chains via a thioester
linkage to a phosphopantetheine prosthetic group as the chains are
elongated. There is also evidence that it has a function in the
biosynthesis of membrane-derived oligosaccharides. Therefore ACP and
its acyl forms interact with at least 12 different E. coli enzymes.
|CITS: [92210530] [89050961] [88296479]| ACP is the most abundant
protein in E. coli, with about 1.5E6 molecules per cell. |CITS: [Mathews&vanHolde]| ACP contains a
phosphopantetheine moiety (as does CoA) as the reactive unit, attached
to the ACP protein through a serine. The holo-ACP synthase enzyme
(encoded by the acpS gene) transfers the 4-phosphopantetheine
moeity of CoA to the apo-ACP to form holo-ACP, which is the active
form of the carrier in lipid synthesis |CITS: [68313114] [81215492]|.)""",
('B1094', 'ACOATA') : """(Lipoate synthase catalyzes the step of lipoic acid biosynthesis at which sulfur is inserted into octanoyl-ACP to form the lipoate moiety |CITS: [8444795], [11106496]|. Lipoate modification (by lipoyl-protein ligases LipB or LplA) of complex subunits is important for function of pyruvate dehydrogenase |CITS: [814874], [6794598], [8444795]|, alpha-ketoglutarate dehydrogenase |CITS: [814874], [6794598], [8444795]|, and the glycine cleavage system |CITS: [1655709], [8444795]|.)""",
('B1094', 'ACOATA') : """(Lipoate synthase catalyzes the step of lipoic acid biosynthesis at which sulfur is inserted into octanoyl-ACP to form the lipoate moiety |CITS: [8444795], [11106496]|. Lipoate synthase is a LipA homodimer with two (4Fe-4S) iron-sulfur clusters per protein dimer under anaerobic conditions, and these clusters are oxidized to the (2Fe-2S) state in air |CITS: [10747808], [10403368]|. The enzyme uses octanoyl-ACP, but not octanoic acid, as substrate and also uses S-adenosyl methionine |CITS: [11106496]|.)""",
('B1094', 'ACOATA') : """NIL""",
('B1094', 'ACOATA') : """NIL""",
('B1094', 'ACOATA') : """NIL""",
('B1094', 'ACOATA') : """NIL""",
('B1094', 'ACOATA') : """NIL""",
('B1094', 'ACOATA') : """NIL""",
('B1094', 'ACOATA') : """NIL""",
('B1094', 'ACOATA') : """NIL""",
('B1094', 'ACOATA') : """NIL""",
('B1094', 'ACOATA') : """NIL""",
('B1094', 'ACOATA') : """NIL""",
('B1094', 'ACOATA') : """NIL""",
('B1094', 'ACOATA') : """NIL""",
('B1094', 'ACOATA') : """NIL""",
('B1094', 'ACOATA') : """NIL""",
('B1094', 'ACOATA') : """NIL""",
('B1094', 'ACOATA') : """(The holo-ACP synthase enzyme (encoded by acpS) transfers the 4-phosphopantetheine
moiety of CoA to the apo-ACP to form holo-ACP, which is the active
form of the carrier in lipid synthesis |CITS: [68313114] [81215492]|.)""",
('B2223', 'ACACt2pp') : """(No information about this protein was found by a literature search conducted on June 13, 2005.
)""",
('B2223', 'HEXt2rpp') : """(No information about this protein was found by a literature search conducted on June 13, 2005.
)""",
('B0521', 'CBMKr') : """(The Pseudomonas aeruginosa ArcC carbamate kinase has been characterized |CITS: [3040889], [2537202]|.)""",
('B0323', 'CBMKr') : """(No information about this protein was found by a literature search
conducted on 23 July 2003.)""",
('B2874', 'CBMKr') : """(No information about this protein was found by a literature search conducted on January 10, 2006.)""",
('B2835', '2AGPE180tipp') : """(LplT is a major facilitator superfamily (MFS) protein that acts as a flippase for transbilayer movement of
lysophospholipids. Mutation experiments and
transporter assays have determined LplT is responsible for the facilitated diffusion of lysophospholipids to
the cytoplasmic portion of the inner membrane providing substrate for the bifunctional enzyme
2-acyl-GPE acyltransferase/acyl-ACP synthetase (Aas). lplT forms an operon with the aas
gene |CITS:[15661733]|.)""",
('B3739', 'ATPS4rpp') : """(A nonpolar mutation in the atpI gene shows that the AtpI protein is not an essential component of the H+-ATPase
complex |CITS: [6327640]|.
Expression of AtpI is 10 to 20-fold lower than expression of AtpB, which is encoded by
the second open reading frame of the atp operon |CITS: [2524469]|. RNA processing and low efficiency of translation
initiation may account for lower levels of atpI transcript and AtpI protein |CITS: [2472380][8679701][1373327][1834655]|.
AtpI appears to affect AtpB expression at a post-translation initiation step |CITS: [7672111]|.)""",
('B2536', 'PPPNt2rpp') : """(HcaT is a member of the major facilitator superfamily (MFS) of transporters |CITS: [98190790]|.
HcaT is a putative 3-phenylpropionate transporter. The hcaT gene is
located immediately downstream of the hcaR gene, whose product regulates
expression of the hcaA-D operon responsible for catabolism of
3-phenylpropionic acid |CITS: [98269008]|.
Membrane topology predictions using experimentally determined C terminus
locations indicate that HcaT has 12 transmembrane helices and the C-terminus is
located in the cytoplasm |CITS:[15044727]|.)""",
('B0650', 'NTP1') : """(HscC (Hsc62) is an E. coli-specific member of the Hsc66 subfamily |CITS: [10574456]| of Hsp70-family
chaperones |CITS: [9735342][12054669]|. Hsc62 exhibits ATPase activity |CITS: [9735342]|, but does not show
chaperone activity toward a denatured protein substrate |CITS: [12183460]|. Hsc62 associates with σ70 and
negatively regulates σ70 activity |CITS: [12059959]|. It is the ATPase domain of Hsc62 that is essential for its
activity towards σ70 |CITS: [14734171]|.
The substrate specificity, substrate binding, and kinetics of ATPase activity have been compared between Hsc62
and DnaK |CITS: [12183460]|. Hsc62 ATPase activity shows a lower optimal temperature than that of Hsc66 and
DnaK, and this ATPase activity is not activated by DnaJ, in contrast to the activation by DnaJ of Hsc66 and DnaK
|CITS: [9735342]|. Hsc62 ATPase activity is activated by the DnaJ-like Hsc56 protein |CITS: [12054669][12183460]|,
whereas the ATPase activity of DnaK or Hsc66 is not activated by Hsc56 |CITS: [12054669]|. Reports differ as to
whether |CITS: [12054669]| or not |CITS: [12183460]| Hsc62 ATPase activity is affected by the GrpE nucleotide
exchange factor.
Overproduction of Hsc62 results in growth inhibition |CITS: [12059959]|. Deletion of Hsc62 also results in growth
inhibition, but this effect wanes after some cell cycles |CITS: [12183460]|. An hscC null mutant exhibits
decreased resistance to Cd2+ stress or to UV light, compared to wild type |CITS: [12183460]|. Hsc62
production does not suppress the phenotypes of a dnaK null mutant |CITS: [12054669][12183460]|. A
dnaK hscA hscC triple null mutant is viable |CITS: [12183460]|. Hsc62 has similarity to DnaK and Hsc66
|CITS: [9735342]|.)""",
('B1325', 'ALAGLUE') : """(YcjG is an L-Ala-D/L-Glu epimerase (of the enolase superfamily) that may act on murein |CITS: [11747447]|. The substrate specificity of the enzyme is not strict |CITS: [11747447]|. Kinetic characterization is performed; the k(cat)/K(M) with L-Ala-D/L-Glu as a substrate is about 10(4) per M per sec|CITS: [11747447]|.
The crystal structure has been determined |CITS: [11747448]|.)""",
('B1064', 'ASR') : """(Glutaredoxins are ubiquitous proteins that catalyze the reduction of disulfides via reduced glutathione (GSH).
Escherichia coli has three glutaredoxins (Grx1, Grx2, and Grx3) containing the classic dithiol active site
CPYC, and a fourth one which contains a monothiol (CGFS) potential active site |CITS: [15833738]|.
The glutaredoxins do not act as enzymes, but rather as a cofactor, enabling intracellular redox reactions through
a disulfide/dithiol enzymatic mechanism involving the active site cysteines.
There is almost no similarity between the amino acid sequence of Grx2 (an approximately 27 kDa protein) and Grx1
or Grx3 (both 9-kDa proteins), with the exception of the active site which is identical in all three glutaredoxins.
In contrast to glutaredoxin 1 and 3, Grx 2 is not a hydrogen donor for ribonucleotide reductase.
On the other hand, Grx2 is the primary hydrogen donor to ArsC-catalyzed arsenate reduction (|FRAME: RXN-982|)
|CITS: [10593884]|. It is also the most abundant glutaredoxin in the cell, with an intracellular concentration
of 5 µM, compared with 0.2 µM and 2.4 µM for Grx1 and 3, respectively |CITS: [10593884]|.)""",
('B1064', 'ASR') : """(Glutaredoxins are ubiquitous proteins that catalyze the reduction of disulfides via reduced glutathione (GSH).
Escherichia coli has three glutaredoxins (Grx1, Grx2, and Grx3) containing the classic dithiol active site
CPYC, and a fourth one which contains a monothiol (CGFS) potential active site |CITS: [15833738]|.
The glutaredoxins do not act as enzymes, but rather as a cofactor, enabling intracellular redox reactions through
a disulfide/dithiol enzymatic mechanism involving the active site cysteines.
There is almost no similarity between the amino acid sequence of Grx2 (an approximately 27 kDa protein) and Grx1
or Grx3 (both 9-kDa proteins), with the exception of the active site which is identical in all three glutaredoxins.
In contrast to glutaredoxin 1 and 3, Grx 2 is not a hydrogen donor for ribonucleotide reductase.
On the other hand, Grx2 is the primary hydrogen donor to ArsC-catalyzed arsenate reduction (|FRAME: RXN-982|)
|CITS: [10593884]|. It is also the most abundant glutaredoxin in the cell, with an intracellular concentration
of 5 µM, compared with 0.2 µM and 2.4 µM for Grx1 and 3, respectively |CITS: [10593884]|.)""",
('B0655', 'ASPabcpp') : """(GltI is the periplasmic-binding component of the GltJKL glutamate ABC transporter |CITS:[10972807],[9593292]|.
gltI was shown to be regulated by the FlhDC flagellar transcriptional regulator |CITS:[15941987]|.
)""",
('B3679', 'INOSTt4pp') : """(The YidK protein is an uncharacterised member of the
SSS superfamily of sodium dependent solute transporters |CITS: [94304911]|.
Based on sequence similarity, YidK may function as a sodium-driven
metabolite uptake system.)""",
('B2045', 'GALKr') : """(WcaK may be involved in colanic acid synthesis based on sequence its
presence in a putative colanic acid synthesis operon |CITS:[8759852]|.
WcaK may be responsible for adding the pyruvyl group to the E ring's
terminal galactosyl residue because it belongs to the polysaccharide
pyruvyl transferase family.)""",
('B2579', 'OBTFL') : """(The yfiD gene encodes a glycyl radical protein that can replace an oxidatively damaged pyruvate formate-lyase subunit |CITS: [11444864]|. YfiD is expected to be involved in stress resistance |CITS: [10726772]|.
Residue Gly102 is predicted to be the glycyl radical site |CITS: [11444864]|. Pyruvate formate-lyase-activase catalyzes YfiD glycyl radical formation |CITS: [11932447]|. Formation of the YfiD glycyl radical is induced by acidic pH (as is yfiD expression) |CITS: [11932447]|. Pyruvate formate-lyase-deactivase does not appear to catalyze YfiD glycyl radical inactivation |CITS: [11932447]|. YfiD is phosphorylated in L-form (wall-less) E. coli |CITS: [9884220]|.
A yfiD mutant shows a defect in acid homeostasis under low-oxygen conditions |CITS: [11932447]|.
YfiD has similarity to pyruvate formate lyase |CITS: [10094700]|.
Regulation has been described |CITS: [9179852], [9767578], [10094700], [10726772], [11114930], [11169114], [11591692], [12107143], [12949096]|.)""",
('B1466', 'NO3R1pp') : """(The polypeptide encoded by narW, the third gene in the narZYWV operon, is not part of the final
nitrate reductase Z enzyme. By similarity to NarJ, it may act as a private chaperone during the incorporation of the
molybdenum cofactor into NarZ, the α subunit of nitrate reductase Z |CITS: [92186712]|.
)""",
('B1226', 'NO3R1pp') : """(NarJ is parto of the redox enzyme maturation protein (REMP) family of chaperones |CITS: [15213747]|. NarJ acts as
a private chaperone during the incorporation of the molybdenum cofactor into NarG, the α subunit of nitrate
reductase A |CITS: [8793883][9305880][9632249][15247236]|.
NarJ, encoded by the third gene in the narGHJI operon, is not part of the final nitrate reductase A enzyme, but
is essential for nitrate reductase activity |CITS: [3053688][92186712][1732220]|. NarJ interacts with the NarG subunit
of the apoenzyme complex at two distinct sites. One site is located at the N terminus of NarG and interferes with
membrane anchoring of the complex |CITS: [16286471][16540088]|, while the second site is involved in the insertion
of the molybdenum cofactor, which precedes membrane anchoring |CITS: [16286471]|. Thus, NarJ appears to
coordinate the final assembly and cofactor acquisition of nitrate reductase A.
Review: |CITS: [15213747]|)""",
('B2963', 'MLTGY1pp') : """(E. coli contains a large number of murein hydrolase enzymes. MltC belongs to the family of lytic
transglycosylases which degrade GlcNAcMurNAc glycan strands, resulting in the formation of a
1,6-anhydro-MurNAc residue at the released product. These enzymes are involved in the cleavage of the septum
during cell division.
Peptidoglycan hydrolase activity of MltC was demonstrated |CITS: [9158737]|.
A mutant containing deletions in mltC, mltD, and mltE has a defect in cell separation, growing as
short chains of cells |CITS: [12399477]|. These chain-forming mutants have a defect in the barrier function of the
outer membrane. A mutant strain lacking all six known lytic transglycosylases (mltA mltB mltC mltD mltE slt) is
unable to induce β-lactamase and is more susceptible to certain high-molecular weight antibiotics which are
normally inactive against Gram-negative bacteria, such as bacitracin, gallidermin and vancomycin |CITS: [15793119]|.
Expression of mltC is induced by oxidative stress via SoxS |CITS: [14594836]|.
Review: |CITS: [7487333]|)""",
('B4392', 'MLTGY1pp') : """(Slt70 is involved in growth and recycling of peptidoglycan by catalyzing
the lysis of the β-1,4 glycosidic bond between N-acetylmuramic
acid and N-acetylglucosamine, producing 1,6-anhydromuropeptides at
an optimal pH of 4.5 with a Km of 200 mg/L |CITS:[357]|.
Slt70 forms a murein-metabolizing multi-enzyme complex with PBP3 and
PBP7/8 |CITS:[8063800]|. PBP7/8 was shown to stabilize and stimulate the
activity of Slt70 |CITS:[8063800]|. Slt70 activity is also modulated by the
stringent response |CITS:[1970319]|.
The structure of Slt70 has been determined by X-ray crystallography
revealing a α-superhelix structure with the catalytic domain on
top |CITS:[2184239],[8107871]|. The structure has also been determined
to a resolution of 1.65 Å for its native form, 1.90 Å as a
complex with 1,6-anhydromuropeptide |CITS:[10452894]|, and 2.8 Å
as a complex with bulgecin A |CITS:[7548026]|, its inhibitor |CITS:[1400320]|.
Overproduction of Slt70 resulted in growth inhibition and lysis of some cells,
but a deletion mutant had no observable phenotype |CITS:[1938883]|.
Review: |CITS:[9529891]|
)""",
('B2813', 'MLTGY1pp') : """(MltA is one of three (along with MltB and Slt70) major lytic endotransglycosylases expressed in Escherichia coli.
MltA and MltB are expressed as membrane-bound lipoproteins. Overexpression of MltA resulted in elevated levels of
a membrane fraction protein with a molecular mass corresponding to the mass of the purified MltA protein |CITS:[8288527]|.
Expression of MltA in cells grown in the presence of H-3 palmitate followed by SDS-PAGE analysis resulted in
fluorographic visualization of a labeled band corresponding to the 39 kDa mass of MltA, demonstrating the lipoprotein
character of MltA |CITS:[6988430]|. Sucrose gradient centrifugation studies have shown that MltA is localized to the
outer membrane |CITS:[9287002]|. Induced overexpression of MltA resulted in lysis of cells grown at 30 degrees Celsius,
the optimal temperature for enzymatic activity, but not at 37 degrees. Furthermore the expressed activity was able to
hydrolyze both murein sacculi as well as isolated glycan strands |CITS:[9287002]|. A triple mltA, mltB, and
slt70 mutant resulted in a 72% reduction in murein turnover |CITS:[10572120]|.)""",
('B2701', 'MLTGY1pp') : """(MltB is one of three (along with MltA and Slt70) major lytic endotransglycosylases expressed in
Escherichia coli. MltA and MltB are expressed as membrane-bound lipoproteins. Expression
of MltB in cells grown in the presence of H-3 palmitate followed by SDS-PAGE analysis resulted in
fluorographic visualization of a labeled band corresponding to the 36 kDa mass of MltB, demonstrating
the lipoprotein character of MltB. Additionally, in the presence of globomycin, an inhibitor of the
lipoprotein signal peptidase, a larger protein, the prolipoprotein form of MltB, was found to accumulate.
Overexpression of mltB resulted in a 55-fold increase in murein hydrolase activity in the membrane
fraction and subsequent cell lysis. Membrane fractionation followed by sucrose-density-gradient
centrifugation indicated that most of the induced hydrolytic activity was located in the outer and
intermediate membrane fractions. A deletion of the mltB gene showed no obvious phenotype
|CITS:[746170]|, while a triple mltA, mltB, and slt70 mutant resulted in a 72%
reduction in murein turnover |CITS:[10572120]|.)""",
('B1193', 'MLTGY1pp') : """(EmtA is a lytic endotransglycosylase which is expressed in Escherichia coli as a membrane-bound lipoprotein.
Overexpression of emtA results in the hydrolysis of glycan strands isolated from the murein (peptidoglycan)
sacculus, which serves as a bacterial exoskeleton |CITS:[9642199]|. It is believed that the emtA gene product,
like other murein hydrolases, is involved in cleavage of the net-like murein structure thereby allowing for cell enlargement
and division and also for localized opening of the peptidoglycan layer to allow the export of bulky compounds such as DNA,
toxins, flagella, and fimbrial proteins |CITS:[8824596]|, |CITS:[9642199]|.)""",
('B1193', 'MLTGY2pp') : """(EmtA is a lytic endotransglycosylase which is expressed in Escherichia coli as a membrane-bound lipoprotein.
Overexpression of emtA results in the hydrolysis of glycan strands isolated from the murein (peptidoglycan)
sacculus, which serves as a bacterial exoskeleton |CITS:[9642199]|. It is believed that the emtA gene product,
like other murein hydrolases, is involved in cleavage of the net-like murein structure thereby allowing for cell enlargement
and division and also for localized opening of the peptidoglycan layer to allow the export of bulky compounds such as DNA,
toxins, flagella, and fimbrial proteins |CITS:[8824596]|, |CITS:[9642199]|.)""",
('B2963', 'MLTGY2pp') : """(E. coli contains a large number of murein hydrolase enzymes. MltC belongs to the family of lytic
transglycosylases which degrade GlcNAcMurNAc glycan strands, resulting in the formation of a
1,6-anhydro-MurNAc residue at the released product. These enzymes are involved in the cleavage of the septum
during cell division.
Peptidoglycan hydrolase activity of MltC was demonstrated |CITS: [9158737]|.
A mutant containing deletions in mltC, mltD, and mltE has a defect in cell separation, growing as
short chains of cells |CITS: [12399477]|. These chain-forming mutants have a defect in the barrier function of the
outer membrane. A mutant strain lacking all six known lytic transglycosylases (mltA mltB mltC mltD mltE slt) is
unable to induce β-lactamase and is more susceptible to certain high-molecular weight antibiotics which are
normally inactive against Gram-negative bacteria, such as bacitracin, gallidermin and vancomycin |CITS: [15793119]|.
Expression of mltC is induced by oxidative stress via SoxS |CITS: [14594836]|.
Review: |CITS: [7487333]|)""",
('B4392', 'MLTGY2pp') : """(Slt70 is involved in growth and recycling of peptidoglycan by catalyzing
the lysis of the β-1,4 glycosidic bond between N-acetylmuramic
acid and N-acetylglucosamine, producing 1,6-anhydromuropeptides at
an optimal pH of 4.5 with a Km of 200 mg/L |CITS:[357]|.
Slt70 forms a murein-metabolizing multi-enzyme complex with PBP3 and
PBP7/8 |CITS:[8063800]|. PBP7/8 was shown to stabilize and stimulate the
activity of Slt70 |CITS:[8063800]|. Slt70 activity is also modulated by the
stringent response |CITS:[1970319]|.
The structure of Slt70 has been determined by X-ray crystallography
revealing a α-superhelix structure with the catalytic domain on
top |CITS:[2184239],[8107871]|. The structure has also been determined
to a resolution of 1.65 Å for its native form, 1.90 Å as a
complex with 1,6-anhydromuropeptide |CITS:[10452894]|, and 2.8 Å
as a complex with bulgecin A |CITS:[7548026]|, its inhibitor |CITS:[1400320]|.
Overproduction of Slt70 resulted in growth inhibition and lysis of some cells,
but a deletion mutant had no observable phenotype |CITS:[1938883]|.
Review: |CITS:[9529891]|
)""",
('B2813', 'MLTGY2pp') : """(MltA is one of three (along with MltB and Slt70) major lytic endotransglycosylases expressed in Escherichia coli.
MltA and MltB are expressed as membrane-bound lipoproteins. Overexpression of MltA resulted in elevated levels of
a membrane fraction protein with a molecular mass corresponding to the mass of the purified MltA protein |CITS:[8288527]|.
Expression of MltA in cells grown in the presence of H-3 palmitate followed by SDS-PAGE analysis resulted in
fluorographic visualization of a labeled band corresponding to the 39 kDa mass of MltA, demonstrating the lipoprotein
character of MltA |CITS:[6988430]|. Sucrose gradient centrifugation studies have shown that MltA is localized to the
outer membrane |CITS:[9287002]|. Induced overexpression of MltA resulted in lysis of cells grown at 30 degrees Celsius,
the optimal temperature for enzymatic activity, but not at 37 degrees. Furthermore the expressed activity was able to
hydrolyze both murein sacculi as well as isolated glycan strands |CITS:[9287002]|. A triple mltA, mltB, and
slt70 mutant resulted in a 72% reduction in murein turnover |CITS:[10572120]|.)""",
('B2701', 'MLTGY2pp') : """(MltB is one of three (along with MltA and Slt70) major lytic endotransglycosylases expressed in
Escherichia coli. MltA and MltB are expressed as membrane-bound lipoproteins. Expression
of MltB in cells grown in the presence of H-3 palmitate followed by SDS-PAGE analysis resulted in
fluorographic visualization of a labeled band corresponding to the 36 kDa mass of MltB, demonstrating
the lipoprotein character of MltB. Additionally, in the presence of globomycin, an inhibitor of the
lipoprotein signal peptidase, a larger protein, the prolipoprotein form of MltB, was found to accumulate.
Overexpression of mltB resulted in a 55-fold increase in murein hydrolase activity in the membrane
fraction and subsequent cell lysis. Membrane fractionation followed by sucrose-density-gradient
centrifugation indicated that most of the induced hydrolytic activity was located in the outer and
intermediate membrane fractions. A deletion of the mltB gene showed no obvious phenotype
|CITS:[746170]|, while a triple mltA, mltB, and slt70 mutant resulted in a 72%
reduction in murein turnover |CITS:[10572120]|.)""",
('B3380', 'PPM') : """(No information about this protein was found by a literature search conducted on December 22, 2005.)""",
('B3127', 'GLYCAt2rpp') : """(YhaU is an uncharacterised member of the major facilitator superfamily (MFS)
of transporters |CITS: [98190790]|.
Based on sequence similarity, YhaU may function as a proton-driven
glucarate uptake system.)""",
('B2789', 'GLYCAt2rpp') : """(The YgcZ protein may function as a glucarate transporter. The
ygcZ gene is encoded in a probable operon with genes
encoding two subunits of a putative glucarate dehydratase. YgcZ
is a member of the major facilitator superfamily (MFS) of
transporters |CITS: [98190790]| and shares a high level of sequence
similarity with probable glucarate transporters from various
organisms. YgcZ probably functions as a glucarate/proton transporter.)""",
('B0957', 'H2Otex') : """(OmpA is a member of the OmpA-OmpF Porin (OOP) family. OmpA is believed to be a nonspecific diffusion channel,
allowing various small solutes to cross the outer membrane. |CITS: [1370823]| It is also believed to serve several other
functions including, as a phage receptor |CITS: [330500]| , as a mediator of F-factor dependent conjugation |CITS: [323051]|,
and in shape stabilization of the bacterium. It is 325 amino acids long and is one of the most abundant proteins in the
outer membrane of E. coli. Structural data at 1.65 angstroms reveals that OmpA consists of an eight-stranded
all-next-neighbor antiparallel beta-barrel. There is some debate asto whether OmpA is truly a channel having both open
and closed conformation |CITS: [7517935]| , or whether the observed porin activity is artifactual.
OmpA was found as a dimer in the outer membrane |CITS:[16079137]|.
Targeting of OmpA to the Sec-translocase for transport across the inner membrane
is SecB-dependent |CITS:[16352602]|.)""",
('B3875', 'H2Otex') : """(OmpL is a member of the OmpG porin Family. It has been shown to localize to the outer membrane and exhibits
porin type properties allowing a non-specific group of solutes smaller than 600 Daltons to pass into and out of
the periplasm. |CITS: [11080145]| Sequence analysis suggests that it has a β-barrel structure consisting
of 12 β-strands. |CITS: [11080145]| It has also been claimed to have an effect on redox potential in the
periplasm |CITS: [11080145]|, however this point is currently contested. |CITS: [12660153]| OmpL also
shows a low, but possibly significant similarity to members of the Cyclodextrin Porin (CDP) family. |CITS: [12192075]|)""",
('B3469', 'NI2abcpp') : """(The gene product of the yhhO gene, also referred to as zntA, is
a P-type ATPase involved in the efflux of Pb(II), Cd(II), and Zn(II) |CITS:[98070750] [20263730]|.
ZntA displays a Km of approximately 20 μM for Cd(II) and
100 μM for Zn(II) |CITS:[20127859]|. The transporter appears to be inhibited
by vanadate, a common inhibitor of P-type ATPase. The ATPase activity of the
transporter was found to follow the order Pb(II), Cd(II), Zn(II), and Hg(II) |CITS:[20127859]|.
A zntA mutant showed hypersensitivity to Cd(II) and Zn(II) |CITS:[98070750]|.
The zntA gene was found to be under the control of the transcriptional
regulator ZntR. zntA expression is activated by an increased concentration
of Cd(II) and Zn(II) within the cell, showing greater induction by Cd(II) than by
Zn(II) |CITS:[20127859]|.)""",
('B0411', 'DURItex') : """(Tsx is a protein involved with the permeation of ribo- and deoxy-nucleosides, across the outer membrane of E. coli.
It also allows the entry of the antibiotic albicidin, and serves as a receptor for bacteriophage and colicins |CITS: [3276691]|
It is believed to form a 14 strand β-barrel porin.
The crystal structure of Tsx has been determined up to 3.1 A co-crystallized with a range of nucleosides |CITS:[15272310]|. Tsx has been shown to localize to the cellular poles |CITS:[15130122]|.)""",
('B0760', 'TUNGSabcpp') : """(ModF is an uncharacterized member of the
ABC superfamily of transporters |CITS: [99091701]|.
It is the putative ATP-binding component of a
transport system whose other members are as yet
unidentified. Based on sequence similarity, this
system may function in the ATP-dependent uptake of
molybdenum.)""",
('B4231', 'RIBabcpp') : """(membrane component of ABC transporter)""",
('B4231', 'RIBabcpp') : """(YtfR, YtfS, YjfF, YtfT, and YtfQ are uncharacterized members
of the ABC superfamily of transporters |CITS: [99091701]|.
YtfR and YtfS are the putative ATP-binding components.
YjfF and YtfT are the putative membrane components.
YtfQ is the putative binding protein. Based on sequence
similarity they probably function together as an ATP-dependant
sugar transporter. The genes ytfR, ytfS, yjfF,
ytfT, and ytfQ probably constitute a single operon.)""",
('B4227', 'RIBabcpp') : """(periplasmic binding component of ABC transporter
YtfQ is upregulated under glucose-limited fed-batch conditions |CITS: [16180237]|.)""",
('B4227', 'RIBabcpp') : """(YtfR, YtfS, YjfF, YtfT, and YtfQ are uncharacterized members
of the ABC superfamily of transporters |CITS: [99091701]|.
YtfR and YtfS are the putative ATP-binding components.
YjfF and YtfT are the putative membrane components.
YtfQ is the putative binding protein. Based on sequence
similarity they probably function together as an ATP-dependant
sugar transporter. The genes ytfR, ytfS, yjfF,
ytfT, and ytfQ probably constitute a single operon.)""",
('B4485', 'RIBabcpp') : """(ATP-binding component of ABC transporter)""",
('B4485', 'RIBabcpp') : """(YtfR, YtfS, YjfF, YtfT, and YtfQ are uncharacterized members
of the ABC superfamily of transporters |CITS: [99091701]|.
YtfR and YtfS are the putative ATP-binding components.
YjfF and YtfT are the putative membrane components.
YtfQ is the putative binding protein. Based on sequence
similarity they probably function together as an ATP-dependant
sugar transporter. The genes ytfR, ytfS, yjfF,
ytfT, and ytfQ probably constitute a single operon.)""",
('B4230', 'RIBabcpp') : """(membrane component of ABC transporter)""",
('B4230', 'RIBabcpp') : """(YtfR, YtfS, YjfF, YtfT, and YtfQ are uncharacterized members
of the ABC superfamily of transporters |CITS: [99091701]|.
YtfR and YtfS are the putative ATP-binding components.
YjfF and YtfT are the putative membrane components.
YtfQ is the putative binding protein. Based on sequence
similarity they probably function together as an ATP-dependant
sugar transporter. The genes ytfR, ytfS, yjfF,
ytfT, and ytfQ probably constitute a single operon.)""",
('B3748', 'RIBabcpp') : """(The RbsD protein is required for efficient utilization of ribose when ribose is transported into the cell via a mutated form
of PtsG, the glucose transporter |CITS: [10318813]|. A mutation in rbsD does not abolish ribose transport
|CITS: [10318813]|.
Utilizing NMR techniques, RbsD was shown to catalyze the conversion of the pyran to the furan form of ribose
|CITS: [15060078]|.
)""",
('B0936', 'MSO3abcpp') : """NIL""",
('B0936', 'MSO3abcpp') : """(Deletion mutation studies |CITS:[10506196]| indicate that the ssuEADCB gene cluster codes for proteins that enable Escherichia coli
to utilize sulfonates other than taurine as a sulfur source. Based on sequence similarity SsuABC is the ABC type transport system with
SsuA being the periplasmic substrate-binding subunit, SsuB the ATP-binding subunit and SsuC the permease. ssuD and
ssuE encode an FMNH2-dependent monooxygenase and an NAD(P)H-dependent FMN reductase, respectively.)""",
('B0933', 'MSO3abcpp') : """(ATP-binding component of ABC transporter)""",
('B0933', 'MSO3abcpp') : """(Deletion mutation studies |CITS:[10506196]| indicate that the ssuEADCB gene cluster codes for proteins that enable Escherichia coli
to utilize sulfonates other than taurine as a sulfur source. Based on sequence similarity SsuABC is the ABC type transport system with
SsuA being the periplasmic substrate-binding subunit, SsuB the ATP-binding subunit and SsuC the permease. ssuD and
ssuE encode an FMNH2-dependent monooxygenase and an NAD(P)H-dependent FMN reductase, respectively.)""",
('B0934', 'MSO3abcpp') : """(membrane component of ABC transporter
Protein topology in the inner membrane has been determined |CITS: [11867724]|.)""",
('B0934', 'MSO3abcpp') : """(Deletion mutation studies |CITS:[10506196]| indicate that the ssuEADCB gene cluster codes for proteins that enable Escherichia coli
to utilize sulfonates other than taurine as a sulfur source. Based on sequence similarity SsuABC is the ABC type transport system with
SsuA being the periplasmic substrate-binding subunit, SsuB the ATP-binding subunit and SsuC the permease. ssuD and
ssuE encode an FMNH2-dependent monooxygenase and an NAD(P)H-dependent FMN reductase, respectively.)""",
('B0572', 'AGt3') : """(CusC is the outer membrane factor for the CusCFBA copper efflux system.
The cusABFCRS gene cluster has similarity to a gene cluster contained on a silver resistance plasmid from a clinical Salmonella isolate |CITS: [12829274]|.
Agr: "Ag(I) resistance" |CITS: [12829274]|.)""",
('B0572', 'AGt3') : """(The Copper transporting efflux system, CusCFBA, is one of at least three systems involved in copper resistance.
CusB is a member of the membrane fusion protein (MFP) family. CusC is the outer membrane factor which forms a channel in the outer membrane.
CusA is the resistance-nodulation-division (RND) permease. CusF is the periplasmic copper binding protein.
The CusCFBA complex may translocate copper from the cytoplasm to the extracellular enviornment across both the inner and outer membrane. Alternatively, the Cus complex
may capture copper in the periplasm and export it outside. Evidence that supports the alternative claim includes the
periplasmic localization of the copper binding protein, CusF, and the assumption that copper access to the RND protein, CusA, may be possible from the cytoplasm as well as the periplasm. |CITS: [12374972]|
)""",
('B0573', 'AGt3') : """(CusF is a periplasmic copper-binding protein that interacts with the CusCBA copper efflux complex. |CITS: [12813074]|
CusF is a pink copper-binding protein. The UV-vis spectrum of copper-containing CusF showed a absorption maximum
around 510 nm, which has not been reported for any other copper proteins. It is believed that CusF may contain a novel
type of copper binding site. |CITS: [12813074]|
The cusABFCRS gene cluster has similarity to a gene cluster contained on a silver resistance plasmid from a clinical Salmonella isolate |CITS: [12829274]|.
Agr: "Ag(I) resistance" |CITS: [12829274]|.)""",
('B0573', 'AGt3') : """(The Copper transporting efflux system, CusCFBA, is one of at least three systems involved in copper resistance.
CusB is a member of the membrane fusion protein (MFP) family. CusC is the outer membrane factor which forms a channel in the outer membrane.
CusA is the resistance-nodulation-division (RND) permease. CusF is the periplasmic copper binding protein.
The CusCFBA complex may translocate copper from the cytoplasm to the extracellular enviornment across both the inner and outer membrane. Alternatively, the Cus complex
may capture copper in the periplasm and export it outside. Evidence that supports the alternative claim includes the
periplasmic localization of the copper binding protein, CusF, and the assumption that copper access to the RND protein, CusA, may be possible from the cytoplasm as well as the periplasm. |CITS: [12374972]|
)""",
('B0574', 'AGt3') : """(CusB is the membrane fusion protein in the CusCFBA copper efflux system. The function of a membrane fusion protein
like CusB may be to bring the outer membrane factor, CusC, closer to the resistance-nodulation-division permease, CusA.
The cusABFCRS gene cluster has similarity to a gene cluster contained on a silver resistance plasmid from a clinical Salmonella isolate |CITS: [12829274]|.
Agr: "Ag(I) resistance" |CITS: [12829274]|.)""",
('B0574', 'AGt3') : """(The Copper transporting efflux system, CusCFBA, is one of at least three systems involved in copper resistance.
CusB is a member of the membrane fusion protein (MFP) family. CusC is the outer membrane factor which forms a channel in the outer membrane.
CusA is the resistance-nodulation-division (RND) permease. CusF is the periplasmic copper binding protein.
The CusCFBA complex may translocate copper from the cytoplasm to the extracellular enviornment across both the inner and outer membrane. Alternatively, the Cus complex
may capture copper in the periplasm and export it outside. Evidence that supports the alternative claim includes the
periplasmic localization of the copper binding protein, CusF, and the assumption that copper access to the RND protein, CusA, may be possible from the cytoplasm as well as the periplasm. |CITS: [12374972]|
)""",
('B1621', 'MALTptspp') : """(contains PTS Enzyme IIB and IIC domains)""",
('B1621', 'MALTptspp') : """(MalX, the maltose-glucose PTS permease, belongs to the functional
superfamily of the phosphoenolpyruvate (PEP)-dependent, sugar
transporting phosphotransferase system (PTS). The PTS transports
and simultaneously phosphorylates its sugar substrates in a process
called group translocation. MalX presumably takes up exogenous
sugar, releasing the phosphate ester into the cell cytoplasm in
preparation for metabolism |CITS: [8246840]|. The overall PTS-mediated phosphoryl
transfer reaction, requiring the two general energy coupling proteins
of the PTS, Enzyme I and HPr, as well as the three domains of
the Enzyme II complex is:
PEP --> Enzyme I(his~~P)
--> HPr(his~~P)
--> IIA(his~~P) -->
IIB(cys~~P) -(IIC)-> sugar-P.
The MalX (Enzyme IICBMal) can use glucose
and maltose as substrates. It may catalyze facilitated diffusion
as well as group translocation |CITS: [1856179]| . The protein presumably functions
with the glucose Enzyme IIA and is homologous to the glucose-
and N-acetylglucosamine-specific Enzyme IICBs. The physiological
function of MalX is not known |CITS: [1856179]|.
)""",
('B3793', 'ECAP2pp') : """(wzyE has been proposed to encode the polymerase involved in the assembly of linear ECA polysaccharide
chains |CITS: [11673418][12618464][12621029]|. A wzyE null mutant was reported to be unable to synthesize
ECA and to accumulate lipid III |CITS: [11673418]|.
A larger open reading frame in this region was originally thought to exist and encode the
4-alpha-L-fucosyltransferase, which is in fact encoded by the gene directly upstream of wzyE, rffT
|CITS: [11673418]|.)""",
('B3793', 'ECAP2pp') : """(The Enterobacterial Common Antigen biosynthesis protein complex is responsible for synthesizing ECA
polysaccharide chains from Lipid III precursors that have been transferred accross the inner membrane.)""",
('B3785', 'ECAP2pp') : """(WzzE is responsible for regulating the length of phosphoglyceride-linked
Enterobacterial Common Antigen (ECAPG) polysaccharide
chains formed from polymerization by WzyE utilizing Lipid III in the periplasm.
Typically, ECAPG chain lengths are 1 to 14 repeats long with
a modal value of 6 or 7. wzzE mutants display a random, non-modal
distribution of ECAPG polysaccharide chain lengths |CITS:[10515954]|.
wzzE has been shown to be required for the synthesis of cyclic ECA
which contains 4 trisaccharide repeat units and is located in the periplasm
|CITS:[16199561]|. WzzE is predicted to form a complex with WzyE and WzxE
|CITS:[16816184]|.)""",
('B3785', 'ECAP2pp') : """(The Enterobacterial Common Antigen biosynthesis protein complex is responsible for synthesizing ECA
polysaccharide chains from Lipid III precursors that have been transferred accross the inner membrane.)""",
('B2223', 'BUTt2rpp') : """(No information about this protein was found by a literature search conducted on June 13, 2005.
)""",
('B2413', 'SULabcpp') : """(A cysZ mutant is deficient in sulfate assimilation |CITS: [6302202]|.)""",
('B0760', 'MOBDabcpp') : """(ModF is an uncharacterized member of the
ABC superfamily of transporters |CITS: [99091701]|.
It is the putative ATP-binding component of a
transport system whose other members are as yet
unidentified. Based on sequence similarity, this
system may function in the ATP-dependent uptake of
molybdenum.)""",
('B0839', 'MDDCP3pp') : """(DacC is a penicillin-binding protein that is required for proper cell morphology and provides
some resistance to penicillin |CITS: [1447130][12354237][6215397]|. It is one of four DD-carboxypeptidase
low-molecular weight PBPs in Escherichia coli (along with PBP4, PBP6 and DacD) that modify
peptidoglycans through the removal of the terminal D-alanine from pentapeptide side chains |CITS:[368033]|,
|CITS:[8955390]|.
The carboxy-terminus of DacC is capable of forming an alpha helix and interacts with
membranes chiefly through hydrophobic forces |CITS: [9371419][9858668]|.
Deletion of this membrane-anchoring portion of the protein produces soluble DacC. Whereas
overexpression of native DacC results in membrane vesicles in the cystoplasm, overexpression
of this soluble variant yields inclusion bodies. Both forms of DacC can be purified with
Procion rubine MX-B and subsequently bind stoichiometrically with penicillin |CITS: [1447130]|.
Despite being part of a family of D-alanine carboxypeptidases, DacC lacks detectable activity
against bisacetyl-L-lysine-D-alanyl-D-alanine and other test substrates |CITS: [1447130]|.
Deletions in dacC are viable, though slightly penicillin sensitive |CITS: [6215397]|.
dacC dacA double mutants are viable, though they show defects in morphology and cell division
when bolA, which is required for dacC expression on entry to stationary phase, is overexpressed |CITS: [3903044][12354237][2684651]|.
A complete deletion of dacA-D is also viable, as is a strain lacking eight of the known penicillin-binding protein genes,
dacC among them |CITS: [8955390][10383966]|. Overexpression of DacC allows cell division in ftsI23 mutants, but leads to cell
lysis during early exponential growth |CITS: [2254246][11325933]|.)""",
('B0484', 'CU1abcpp') : """(YbaR is an uncharacterized member of the P-type ATPase cation transporter family |CITS:[94202222]|.
Based on sequence similarity, it may function as a copper transporting ATPase.)""",
}