category3_ecocyc_comments_of_gene = {('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]|.)""",
('B0732', 'MANPGH') : """(The mngB gene encodes an alpha-mannosidase |CITS: [14645248]|.)""",
('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]|)""",
('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]|.)""",
('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]|.)""",
('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]|.)""",
('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]|.)""",
('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]|.)""",
('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]|.)""",
('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]|.)""",
('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]|.)""",
('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]|)""",
('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]|.)""",
('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]|)""",
('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]|)""",
('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]|.)""",
('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]|.)""",
('B2033', 'O16AT') : """(No information about this protein was found by a literature search
conducted on February 26, 2004.)""",
('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]|)""",
('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.)""",
('B2523', 'AMPTASEPG') : """(The pepB gene encodes an aminopeptidase (AP) |CITS: [372108]|.)""",
('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]|.)""",
('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.)""",
('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]|.)""",
('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]|.)""",
('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]|.)""",
('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]|.)""",
('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.)""",
('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]|.)""",
('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]|.)""",
('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]|.)""",
('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]|.)""",
('B2523', 'AMPTASECG') : """(The pepB gene encodes an aminopeptidase (AP) |CITS: [372108]|.)""",
('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]|.)""",
('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]|)""",
('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]|.)""",
('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]|.)""",
('B2032', 'O16GLCT1') : """(No information about this protein was found by a literature search conducted on November 29, 2005.)""",
('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]|.)""",
('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]|.)""",
('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]|.)""",
('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]|.)""",
('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]|.)""",
('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]|.)""",
('B4358', 'GALCTLO') : """(YjjN did not show dehydrogenase activity in a high-throughput screen of purified proteins |CITS: [15808744]|.
)""",
('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]|.)""",
('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]|.)""",
}