category4_ecocyc_comments_of_gene = {('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]|. )""", ('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]|.)""", ('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]|)""", ('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.)""", ('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.)""", ('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]|.)""", ('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]|.)""", ('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.)""", ('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]|.)""", ('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]|.)""", ('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. )""", ('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]|.)""", ('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]|.)""", ('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]|.)""", ('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]|.)""", ('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]|. )""", ('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.)""", ('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]|.)""", ('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.)""", ('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]|.)""", ('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]|.)""", ('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.)""", ('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]|.)""", ('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]|.)""", ('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.)""", ('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]|.)""", ('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]|)""", ('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]|.)""", ('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""", ('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.)""", ('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]|.)""", ('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]|.)""", ('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]|.)""", ('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]| )""", ('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]|.)""", ('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]|.)""", ('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.)""", ('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]|.)""", ('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]|.)""", ('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]| )""", ('B2690', 'PGMT') : """(Phosphatase activity of YqaB was discovered in a high-throughput screen of purified proteins |CITS: [15808744]|. )""", ('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]|.
)""", ('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]|.)""", ('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.)""", ('B2223', 'BUTt2rpp') : """(No information about this protein was found by a literature search conducted on June 13, 2005. )""", ('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]|.)""", ('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]|.)""", ('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]|.)""", ('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]|.)""", ('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]|)""", ('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]|.)""", ('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]|)""", ('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.)""", }