comments_of_protein_by_blattner = {('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). <I>lplT</I> forms an operon with the <I>aas</I> gene |CITS:[15661733]|.)""", ('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). <I>lplT</I> forms an operon with the <I>aas</I> gene |CITS:[15661733]|.)""", ('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). <I>lplT</I> forms an operon with the <I>aas</I> 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). <I>lplT</I> forms an operon with the <I>aas</I> gene |CITS:[15661733]|.)""", ('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). <I>lplT</I> forms an operon with the <I>aas</I> gene |CITS:[15661733]|.)""", ('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). <I>lplT</I> forms an operon with the <I>aas</I> gene |CITS:[15661733]|.)""", ('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). <I>lplT</I> forms an operon with the <I>aas</I> gene |CITS:[15661733]|.)""", ('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). <I>lplT</I> forms an operon with the <I>aas</I> gene |CITS:[15661733]|.)""", ('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). <I>lplT</I> forms an operon with the <I>aas</I> gene |CITS:[15661733]|.)""", ('B2223', 'ACACt2pp') :  """(No information about this protein was found by a literature search conducted on June 13, 2005. )""", ('B0411', 'ADNtex') :  """(Tsx is a protein involved with the permeation of ribo- and deoxy-nucleosides, across the outer membrane of <I>E. coli</I>.  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 &beta;-barrel porin.  The crystal structure of Tsx has been determined up to 3.1 A co-crystallized with a range of nucleosides |CITS:[15272310]|. Tsx has been shown to localize to the cellular poles |CITS:[15130122]|.)""", ('B0511', 'ALLTNt2rpp') :  """(The YbbW protein is an uncharacterized member of the  NCS1 family of purine and pyrimidine transporters  |CITS: [99184734]|. Based on sequence similarity,  YbbW may function as a proton-driven allantoin uptake  system. Supporting this notion, the downstream gene  from <I>ybbW</I> encodes a putative allantoinase enzyme.)""", ('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 <i>Salmonella typhimurium</i> SE5312 mutant |CITS: [8344936]|.  CutE overproduction in <i>Salmonella typhimurium</i> results in increased apolipoprotein N-acyltransferase activity |CITS: [8344936]|.  CutE has similarity to <i>Rhizobium meliloti</i> 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 <I>Escherichia coli</I> |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]|.)""", ('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 <i>Salmonella typhimurium</i> SE5312 mutant |CITS: [8344936]|.  CutE overproduction in <i>Salmonella typhimurium</i> results in increased apolipoprotein N-acyltransferase activity |CITS: [8344936]|.  CutE has similarity to <i>Rhizobium meliloti</i> 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 <I>Escherichia coli</I> |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]|.)""", ('B1605', 'ARGORNt7pp') :  """(ArcD is an uncharacterised member of the APC family of  amino acid transporters. ArcD is highly similar to the  <I>Pseudomonas aeruginosa</I> ArcD arginine/ornithine  antiporter and probably has a similar function.)""", ('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]|)""", ('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 <i>ulaG</i> is negatively regulated by UlaR |CITS: [12374842]|.)""", ('B2223', 'BUTt2rpp') :  """(No information about this protein was found by a literature search conducted on June 13, 2005. )""", ('B3469', 'CD2abcpp') :  """(The gene product of the <I>yhhO</I> gene, also referred to as <I>zntA</I>, is a P-type ATPase involved in the efflux of Pb(II), Cd(II), and Zn(II) |CITS:[98070750] [20263730]|.  ZntA displays a K<sub>m</sub> of approximately 20 &mu;M for Cd(II) and  100 &mu;M 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 <I>zntA</I> mutant showed hypersensitivity to Cd(II) and Zn(II) |CITS:[98070750]|.  The <I>zntA</I> gene was found to be under the control of the transcriptional  regulator ZntR. <I>zntA</I> 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', '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 <I>yehX</I>, <I>yehW</I>,  <I>yehY</I>, and <I>yehZ</I> genes are located  within a single operon.  Osmotic shock and entry into stationary phase induced transcription of the <I>yehZYXW</I> operon, which was dependent upon &sigma;<sup>s</sup> |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 <I>yehX</I>, <I>yehW</I>,  <I>yehY</I>, and <I>yehZ</I> genes are located  within a single operon.  Osmotic shock and entry into stationary phase induced transcription of the <I>yehZYXW</I> operon, which was dependent upon &sigma;<sup>s</sup> |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 <I>yehX</I>, <I>yehW</I>,  <I>yehY</I>, and <I>yehZ</I> genes are located  within a single operon.  Osmotic shock and entry into stationary phase induced transcription of the <I>yehZYXW</I> operon, which was dependent upon &sigma;<sup>s</sup> |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 <I>yehX</I>, <I>yehW</I>,  <I>yehY</I>, and <I>yehZ</I> genes are located  within a single operon.  Osmotic shock and entry into stationary phase induced transcription of the <I>yehZYXW</I> operon, which was dependent upon &sigma;<sup>s</sup> |CITS:[15251200]|.)""", ('B3469', 'COBALT2abcpp') :  """(The gene product of the <I>yhhO</I> gene, also referred to as <I>zntA</I>, is a P-type ATPase involved in the efflux of Pb(II), Cd(II), and Zn(II) |CITS:[98070750] [20263730]|.  ZntA displays a K<sub>m</sub> of approximately 20 &mu;M for Cd(II) and  100 &mu;M 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 <I>zntA</I> mutant showed hypersensitivity to Cd(II) and Zn(II) |CITS:[98070750]|.  The <I>zntA</I> gene was found to be under the control of the transcriptional  regulator ZntR. <I>zntA</I> 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]|.)""", ('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.)""", ('B3469', 'CU2abcpp') :  """(The gene product of the <I>yhhO</I> gene, also referred to as <I>zntA</I>, is a P-type ATPase involved in the efflux of Pb(II), Cd(II), and Zn(II) |CITS:[98070750] [20263730]|.  ZntA displays a K<sub>m</sub> of approximately 20 &mu;M for Cd(II) and  100 &mu;M 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 <I>zntA</I> mutant showed hypersensitivity to Cd(II) and Zn(II) |CITS:[98070750]|.  The <I>zntA</I> gene was found to be under the control of the transcriptional  regulator ZntR. <I>zntA</I> expression is activated by an increased concentration  of Cd(II) and Zn(II) within the cell, showing greater induction by Cd(II)  than by  Zn(II) |CITS:[20127859]|.)""", ('B0411', 'DADNtex') :  """(Tsx is a protein involved with the permeation of ribo- and deoxy-nucleosides, across the outer membrane of <I>E. coli</I>.  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 &beta;-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 <I>E. coli</I>.  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 &beta;-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', 'DURItex') :  """(Tsx is a protein involved with the permeation of ribo- and deoxy-nucleosides, across the outer membrane of <I>E. coli</I>.  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 &beta;-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]|.)""", ('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.)""", ('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 <i>frlA</i> mutant is unable to grow on 20mM fructoselysine or psicoselysine as the sole source of carbon |CITS: [14641112]|.  FrlA: "fructoselysine" |CITS: [12147680]|.)""", ('B2789', 'GALCTt2rpp') :  """(The YgcZ protein may function as a glucarate transporter. The  <I>ygcZ</I> 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.)""", ('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  <I>ygcZ</I> 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.)""", ('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 <I>yehX</I>, <I>yehW</I>,  <I>yehY</I>, and <I>yehZ</I> genes are located  within a single operon.  Osmotic shock and entry into stationary phase induced transcription of the <I>yehZYXW</I> operon, which was dependent upon &sigma;<sup>s</sup> |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 <I>yehX</I>, <I>yehW</I>,  <I>yehY</I>, and <I>yehZ</I> genes are located  within a single operon.  Osmotic shock and entry into stationary phase induced transcription of the <I>yehZYXW</I> operon, which was dependent upon &sigma;<sup>s</sup> |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 <I>yehX</I>, <I>yehW</I>,  <I>yehY</I>, and <I>yehZ</I> genes are located  within a single operon.  Osmotic shock and entry into stationary phase induced transcription of the <I>yehZYXW</I> operon, which was dependent upon &sigma;<sup>s</sup> |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 <I>yehX</I>, <I>yehW</I>,  <I>yehY</I>, and <I>yehZ</I> genes are located  within a single operon.  Osmotic shock and entry into stationary phase induced transcription of the <I>yehZYXW</I> operon, which was dependent upon &sigma;<sup>s</sup> |CITS:[15251200]|.)""", ('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  <I>ygcZ</I> 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.)""", ('B2979', 'GLYCTO2') :  """(<i>E. coli</i> cells harboring a plasmid containing <i>glcDEF</i> have glycolate oxidase activity in crude cell extracts; an insertion mutant in either <i>glcD</i>, <i>glcE</i> or <i>glcF</i> abolishes this activity |CITS: [8606183]|.)""", ('B4467', 'GLYCTO2') :  """(<i>E. coli</i> cells harboring a plasmid containing <i>glcDEF</i> have glycolate oxidase activity in crude cell extracts; an insertion mutant in either <i>glcD</i>, <i>glcE</i> or <i>glcF</i> abolishes this activity |CITS: [8606183]|.)""", ('B4468', 'GLYCTO2') :  """(<i>E. coli</i> cells harboring a plasmid containing <i>glcDEF</i> have glycolate oxidase activity in crude cell extracts; an insertion mutant in either <i>glcD</i>, <i>glcE</i> or <i>glcF</i> abolishes this activity |CITS: [8606183]|.)""", ('B2979', 'GLYCTO3') :  """(<i>E. coli</i> cells harboring a plasmid containing <i>glcDEF</i> have glycolate oxidase activity in crude cell extracts; an insertion mutant in either <i>glcD</i>, <i>glcE</i> or <i>glcF</i> abolishes this activity |CITS: [8606183]|.)""", ('B4467', 'GLYCTO3') :  """(<i>E. coli</i> cells harboring a plasmid containing <i>glcDEF</i> have glycolate oxidase activity in crude cell extracts; an insertion mutant in either <i>glcD</i>, <i>glcE</i> or <i>glcF</i> abolishes this activity |CITS: [8606183]|.)""", ('B4468', 'GLYCTO3') :  """(<i>E. coli</i> cells harboring a plasmid containing <i>glcDEF</i> have glycolate oxidase activity in crude cell extracts; an insertion mutant in either <i>glcD</i>, <i>glcE</i> or <i>glcF</i> abolishes this activity |CITS: [8606183]|.)""", ('B2979', 'GLYCTO4') :  """(<i>E. coli</i> cells harboring a plasmid containing <i>glcDEF</i> have glycolate oxidase activity in crude cell extracts; an insertion mutant in either <i>glcD</i>, <i>glcE</i> or <i>glcF</i> abolishes this activity |CITS: [8606183]|.)""", ('B4467', 'GLYCTO4') :  """(<i>E. coli</i> cells harboring a plasmid containing <i>glcDEF</i> have glycolate oxidase activity in crude cell extracts; an insertion mutant in either <i>glcD</i>, <i>glcE</i> or <i>glcF</i> abolishes this activity |CITS: [8606183]|.)""", ('B4468', 'GLYCTO4') :  """(<i>E. coli</i> cells harboring a plasmid containing <i>glcDEF</i> have glycolate oxidase activity in crude cell extracts; an insertion mutant in either <i>glcD</i>, <i>glcE</i> or <i>glcF</i> abolishes this activity |CITS: [8606183]|.)""", ('B0411', 'GUAtex') :  """(Tsx is a protein involved with the permeation of ribo- and deoxy-nucleosides, across the outer membrane of <I>E. coli</I>.  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 &beta;-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]|.)""", ('B2223', 'HEXt2rpp') :  """(No information about this protein was found by a literature search conducted on June 13, 2005. )""", ('B3469', 'HG2abcpp') :  """(The gene product of the <I>yhhO</I> gene, also referred to as <I>zntA</I>, is a P-type ATPase involved in the efflux of Pb(II), Cd(II), and Zn(II) |CITS:[98070750] [20263730]|.  ZntA displays a K<sub>m</sub> of approximately 20 &mu;M for Cd(II) and  100 &mu;M 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 <I>zntA</I> mutant showed hypersensitivity to Cd(II) and Zn(II) |CITS:[98070750]|.  The <I>zntA</I> gene was found to be under the control of the transcriptional  regulator ZntR. <I>zntA</I> 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]|.)""", ('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.)""", ('B0411', 'INStex') :  """(Tsx is a protein involved with the permeation of ribo- and deoxy-nucleosides, across the outer membrane of <I>E. coli</I>.  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 &beta;-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]|.)""", ('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]|)""", ('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]|)""", ('B0936', 'MSO3abcpp') :  """NIL""", ('B0936', 'MSO3abcpp') :  """(Deletion mutation studies |CITS:[10506196]| indicate that the <I>ssuEADCB</I> 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.   <I>ssuD</I> and  <I>ssuE</I> 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 <I>ssuEADCB</I> 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.   <I>ssuD</I> and  <I>ssuE</I> 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 <I>ssuEADCB</I> 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.   <I>ssuD</I> and  <I>ssuE</I> encode an FMNH2-dependent monooxygenase and an NAD(P)H-dependent FMN reductase, respectively.)""", ('B3469', 'NI2abcpp') :  """(The gene product of the <I>yhhO</I> gene, also referred to as <I>zntA</I>, is a P-type ATPase involved in the efflux of Pb(II), Cd(II), and Zn(II) |CITS:[98070750] [20263730]|.  ZntA displays a K<sub>m</sub> of approximately 20 &mu;M for Cd(II) and  100 &mu;M 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 <I>zntA</I> mutant showed hypersensitivity to Cd(II) and Zn(II) |CITS:[98070750]|.  The <I>zntA</I> gene was found to be under the control of the transcriptional  regulator ZntR. <I>zntA</I> 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]|.)""", ('B2536', 'PPPNt2rpp') :  """(HcaT is a member of the major facilitator superfamily (MFS) of transporters |CITS: [98190790]|. HcaT is a putative 3-phenylpropionate transporter. The <I>hcaT</I> gene is  located immediately downstream of the <I>hcaR</I> gene, whose product regulates  expression of the <I>hcaA-D</I> 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]|.)""", ('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 <i>frlA</i> 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 <I>ssuEADCB</I> 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.   <I>ssuD</I> and  <I>ssuE</I> 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 <I>ssuEADCB</I> 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.   <I>ssuD</I> and  <I>ssuE</I> 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 <I>ssuEADCB</I> 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.   <I>ssuD</I> and  <I>ssuE</I> 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 <I>E. coli</I>.  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 &beta;-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]|.)""", ('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 <I>yiaMNO</I> genes encode the only tri-partite ATP-independent periplasmic (TRAP) transporter in <I>Escherichia coli</I>.  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 <I>yiaMNO</I> genes affected the ability of <I>E.coli</I> to utilize L-xylulose when  growth was measured using various carbon substrates.  Solute transport studies |CITS:[14668138]| determined that the <I>yiaMNO</I> 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 <I>yiaMNO</I> 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 OD<sub>660</sub> and higher c.f.u. numbers. Deletion of <I>yiaMNO</I> 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 <I>yiaMNO</I> genes encode the only tri-partite ATP-independent periplasmic (TRAP) transporter in <I>Escherichia coli</I>.  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 <I>yiaMNO</I> genes affected the ability of <I>E.coli</I> to utilize L-xylulose when  growth was measured using various carbon substrates.  Solute transport studies |CITS:[14668138]| determined that the <I>yiaMNO</I> 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 <I>yiaMNO</I> 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 OD<sub>660</sub> and higher c.f.u. numbers. Deletion of <I>yiaMNO</I> 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 <I>yiaMNO</I> genes encode the only tri-partite ATP-independent periplasmic (TRAP) transporter in <I>Escherichia coli</I>.  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 <I>yiaMNO</I> genes affected the ability of <I>E.coli</I> to utilize L-xylulose when  growth was measured using various carbon substrates.  Solute transport studies |CITS:[14668138]| determined that the <I>yiaMNO</I> 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 <I>yiaMNO</I> 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 OD<sub>660</sub> and higher c.f.u. numbers. Deletion of <I>yiaMNO</I> 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]|.)""", }