Penicillin-binding protein 1B

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

Miscellaneous

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityⁱ

• [GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)]_(n)-diphospho-di-trans,octa-cis-undecaprenol

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.

  + β-D-GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-di-trans,octa-cis-undecaprenol

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  = [GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)]_(n+1)-diphospho-di-trans-octa-cis-undecaprenol

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.

  + di-trans,octa-cis-undecaprenyl diphosphate

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  + H⁺

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  2 Publications

  <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment inⁱ

  • Ref.6

    "Functional biosynthesis of cell wall peptidoglycan by polymorphic bifunctional polypeptides. Penicillin-binding protein 1Bs of Escherichia coli with activities of transglycosylase and transpeptidase."
    Nakagawa J., Tamaki S., Tomioka S., Matsuhashi M.
    J. Biol. Chem. 259:13937-13946(1984) [PubMed] [Europe PMC] [Abstract]

    Cited for: CATALYTIC ACTIVITY.
  • Ref.14

    "Crystal structure of the membrane-bound bifunctional transglycosylase PBP1b from Escherichia coli."
    Sung M.-T., Lai Y.-T., Huang C.-Y., Chou L.-Y., Shih H.-W., Cheng W.-C., Wong C.-H., Ma C.
    Proc. Natl. Acad. Sci. U.S.A. 106:8824-8829(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.16 ANGSTROMS) OF 58-804 IN COMPLEX WITH MOENOMYCIN, PARTIAL PROTEIN SEQUENCE, INTERACTION WITH MLTA; UVRA; FTSL AND FTSN, MEMBRANE TOPOLOGY, CATALYTIC ACTIVITY, DOMAIN, IDENTIFICATION BY MASS SPECTROMETRY.
  EC:2.4.1.129
  • Search proteins in UniProtKB for this EC number.
  • See the description of this EC number in ENZYME.
  2 Publications

  Manual assertion based on experiment inⁱ

  • Ref.6

    "Functional biosynthesis of cell wall peptidoglycan by polymorphic bifunctional polypeptides. Penicillin-binding protein 1Bs of Escherichia coli with activities of transglycosylase and transpeptidase."
    Nakagawa J., Tamaki S., Tomioka S., Matsuhashi M.
    J. Biol. Chem. 259:13937-13946(1984) [PubMed] [Europe PMC] [Abstract]

    Cited for: CATALYTIC ACTIVITY.
  • Ref.14

    "Crystal structure of the membrane-bound bifunctional transglycosylase PBP1b from Escherichia coli."
    Sung M.-T., Lai Y.-T., Huang C.-Y., Chou L.-Y., Shih H.-W., Cheng W.-C., Wong C.-H., Ma C.
    Proc. Natl. Acad. Sci. U.S.A. 106:8824-8829(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.16 ANGSTROMS) OF 58-804 IN COMPLEX WITH MOENOMYCIN, PARTIAL PROTEIN SEQUENCE, INTERACTION WITH MLTA; UVRA; FTSL AND FTSN, MEMBRANE TOPOLOGY, CATALYTIC ACTIVITY, DOMAIN, IDENTIFICATION BY MASS SPECTROMETRY.
  Source: Rhea

  • Search for this reaction in UniProtKB.
  • See the description of this reaction in Rhea.

  . Show »« Hide
  [GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)]_(n)-diphospho-di-trans,octa-cis-undecaprenol

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.

  zoom

  +

  β-D-GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-di-trans,octa-cis-undecaprenol

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  zoom

  =

  [GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)]_(n+1)-diphospho-di-trans-octa-cis-undecaprenol

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.

  zoom

  +

  di-trans,octa-cis-undecaprenyl diphosphate

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  zoom

  +

  H⁺

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  

• Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.1 Publication

  Manual assertion based on experiment inⁱ

  • Ref.6

    "Functional biosynthesis of cell wall peptidoglycan by polymorphic bifunctional polypeptides. Penicillin-binding protein 1Bs of Escherichia coli with activities of transglycosylase and transpeptidase."
    Nakagawa J., Tamaki S., Tomioka S., Matsuhashi M.
    J. Biol. Chem. 259:13937-13946(1984) [PubMed] [Europe PMC] [Abstract]

    Cited for: CATALYTIC ACTIVITY.

  EC:3.4.16.4

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• drug binding Source: EcoCyc <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • Ref.12

    "The catalytic, glycosyl transferase and acyl transferase modules of the cell wall peptidoglycan-polymerizing penicillin-binding protein 1b of Escherichia coli."
    Terrak M., Ghosh T.K., van Heijenoort J., Van Beeumen J., Lampilas M., Aszodi J., Ayala J.A., Ghuysen J.-M., Nguyen-Disteche M.
    Mol. Microbiol. 34:350-364(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: ACTIVE SITE SER-510, MUTAGENESIS OF GLU-233; ASP-234 AND GLU-290.
  • "Moenomycin-mediated affinity purification of penicillin-binding protein 1b."
    Stembera K., Buchynskyy A., Vogel S., Knoll D., Osman A.A., Ayala J.A., Welzel P.
    Chembiochem 3:332-340(2002) [PubMed] [Europe PMC] [Abstract]
  • "A surface plasmon resonance analysis of the interaction between the antibiotic moenomycin A and penicillin-binding protein 1b."
    Stembera K., Vogel S., Buchynskyy A., Ayala J.A., Welzel P.
    Chembiochem 3:559-565(2002) [PubMed] [Europe PMC] [Abstract]
  • "New cephamycin antibiotic, CS-1170: binding affinity to penicillin-binding proteins and inhibition of peptidoglycan cross-linking reactions in Escherichia coli."
    Ohya S., Yamazaki M., Sugawara S., Tamaki S., Matsuhashi M.
    Antimicrob. Agents Chemother. 14:780-785(1978) [PubMed] [Europe PMC] [Abstract]
  • "SCE-963, a new potent cephalosporin with high affinity for penicillin-binding proteins 1 and 3 of Escherichia coli."
    Nozaki Y., Imada A., Yoneda M.
    Antimicrob. Agents Chemother. 15:20-27(1979) [PubMed] [Europe PMC] [Abstract]
  • "Cefotaxime: binding affinity to penicillin-binding proteins and morphological changes of Escherichia coli and Pseudomonas aeruginosa."
    Masuyoshi S., Inoue M., Takaoka M., Mitsuhashi S.
    Arzneimittelforschung 31:1070-1072(1981) [PubMed] [Europe PMC] [Abstract]
  • "Binding of 125I-labeled beta-lactam antibiotics to the penicillin binding proteins of Escherichia coli."
    Rojo F., Ayala J.A., de la Rosa E.J., de Pedro M.A., Aran V., Berenguer J., Vazquez D.
    J. Antibiot. 37:389-393(1984) [PubMed] [Europe PMC] [Abstract]
  • "Affinity of cefonicid, a long-acting cephalosporin, for the penicillin-binding proteins of Escherichia coli K-12."
    Rake J.B., Newman D.J., Actor P.
    J. Antibiot. 37:572-576(1984) [PubMed] [Europe PMC] [Abstract]
  • "Studies on the mechanism of action of imipenem (N-formimidoylthienamycin) in vitro: binding to the penicillin-binding proteins (PBPs) in Escherichia coli and Pseudomonas aeruginosa, and inhibition of enzyme activities due to the PBPs in E. coli."
    Hashizume T., Ishino F., Nakagawa J., Tamaki S., Matsuhashi M.
    J. Antibiot. 37:394-400(1984) [PubMed] [Europe PMC] [Abstract]
  • "Affinity of cefoperazone for penicillin-binding proteins."
    Matsubara N., Minami S., Matsuhashi M., Takaoka M., Mitsuhashi S.
    Antimicrob. Agents Chemother. 18:195-199(1980) [PubMed] [Europe PMC] [Abstract]
  • "Moxalactam (6059-S), a new 1-oxa-beta-lactam: binding affinity for penicillin-binding proteins of Escherichia coli K-12."
    Komatsu Y., Nishikawa T.
    Antimicrob. Agents Chemother. 17:316-321(1980) [PubMed] [Europe PMC] [Abstract]
  • "Cefmenoxime (SCE-1365), a novel broad-spectrum cephalosporin: in vitro and in vivo antibacterial activities."
    Tsuchiya K., Kondo M., Kida M., Nakao M., Iwahi T., Nishi T., Noji Y., Takeuchi M., Nozaki Y.
    Antimicrob. Agents Chemother. 19:56-65(1981) [PubMed] [Europe PMC] [Abstract]
  • "Differences between ceftizoxime and its stereoisomer in antibacterial activity and affinity for penicillin-binding proteins."
    Shigi Y., Kojo H., Wakasugi M., Nishida M.
    Antimicrob. Agents Chemother. 19:393-396(1981) [PubMed] [Europe PMC] [Abstract]
  • "Penem derivatives: beta-lactamase stability and affinity for penicillin-binding proteins in Escherichia coli."
    Ohya S., Utsui Y., Sugawara S., Yamazaki M.
    Antimicrob. Agents Chemother. 21:492-497(1982) [PubMed] [Europe PMC] [Abstract]
• lipopeptide binding Source: EcoCyc <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • "Site-Specific Immobilization of the Peptidoglycan Synthase PBP1B on a Surface Plasmon Resonance Chip Surface."
    Van't Veer I.L., Leloup N.O., Egan A.J., Janssen B.J., Martin N.I., Vollmer W., Breukink E.
    Chembiochem 17:2250-2256(2016) [PubMed] [Europe PMC] [Abstract]
• penicillin binding Source: EcoCycInferred from direct assayⁱ
  • Ref.12

    "The catalytic, glycosyl transferase and acyl transferase modules of the cell wall peptidoglycan-polymerizing penicillin-binding protein 1b of Escherichia coli."
    Terrak M., Ghosh T.K., van Heijenoort J., Van Beeumen J., Lampilas M., Aszodi J., Ayala J.A., Ghuysen J.-M., Nguyen-Disteche M.
    Mol. Microbiol. 34:350-364(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: ACTIVE SITE SER-510, MUTAGENESIS OF GLU-233; ASP-234 AND GLU-290.
  • "On the process of cellular division in Escherichia coli: a series of mutants of E. coli altered in the penicillin-binding proteins."
    Suzuki H., Nishimura Y., Hirota Y.
    Proc. Natl. Acad. Sci. U.S.A. 75:664-668(1978) [PubMed] [Europe PMC] [Abstract]
• peptidoglycan glycosyltransferase activity Source: EcoCycInferred from direct assayⁱ
  • Ref.12

    "The catalytic, glycosyl transferase and acyl transferase modules of the cell wall peptidoglycan-polymerizing penicillin-binding protein 1b of Escherichia coli."
    Terrak M., Ghosh T.K., van Heijenoort J., Van Beeumen J., Lampilas M., Aszodi J., Ayala J.A., Ghuysen J.-M., Nguyen-Disteche M.
    Mol. Microbiol. 34:350-364(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: ACTIVE SITE SER-510, MUTAGENESIS OF GLU-233; ASP-234 AND GLU-290.
  • "Lipid II: total synthesis of the bacterial cell wall precursor and utilization as a substrate for glycosyltransfer and transpeptidation by penicillin binding protein (PBP) 1b of Escherichia coli."
    Schwartz B., Markwalder J.A., Wang Y.
    J. Am. Chem. Soc. 123:11638-11643(2001) [PubMed] [Europe PMC] [Abstract]
  • "A kinetic characterization of the glycosyltransferase activity of Eschericia coli PBP1b and development of a continuous fluorescence assay."
    Schwartz B., Markwalder J.A., Seitz S.P., Wang Y., Stein R.L.
    Biochemistry 41:12552-12561(2002) [PubMed] [Europe PMC] [Abstract]
  • "Vancomycin analogues active against vanA-resistant strains inhibit bacterial transglycosylase without binding substrate."
    Chen L., Walker D., Sun B., Hu Y., Walker S., Kahne D.
    Proc. Natl. Acad. Sci. U.S.A. 100:5658-5663(2003) [PubMed] [Europe PMC] [Abstract]
  • "High-throughput screen for inhibitors of transglycosylase and/or transpeptidase activities of Escherichia coli penicillin binding protein 1b."
    Chandrakala B., Shandil R.K., Mehra U., Ravishankar S., Kaur P., Usha V., Joe B., deSousa S.M.
    Antimicrob. Agents Chemother. 48:30-40(2004) [PubMed] [Europe PMC] [Abstract]
  • "Glycosyl transferase activity of the Escherichia coli penicillin-binding protein 1b: specificity profile for the substrate."
    Fraipont C., Sapunaric F., Zervosen A., Auger G., Devreese B., Lioux T., Blanot D., Mengin-Lecreulx D., Herdewijn P., Van Beeumen J., Frere J.M., Nguyen-Disteche M.
    Biochemistry 45:4007-4013(2006) [PubMed] [Europe PMC] [Abstract]
  • "Screen for inhibitors of the coupled transglycosylase-transpeptidase of peptidoglycan biosynthesis in Escherichia coli."
    Ramachandran V., Chandrakala B., Kumar V.P., Usha V., Solapure S.M., de Sousa S.M.
    Antimicrob. Agents Chemother. 50:1425-1432(2006) [PubMed] [Europe PMC] [Abstract]
  • Ref.6

    "Functional biosynthesis of cell wall peptidoglycan by polymorphic bifunctional polypeptides. Penicillin-binding protein 1Bs of Escherichia coli with activities of transglycosylase and transpeptidase."
    Nakagawa J., Tamaki S., Tomioka S., Matsuhashi M.
    J. Biol. Chem. 259:13937-13946(1984) [PubMed] [Europe PMC] [Abstract]

    Cited for: CATALYTIC ACTIVITY.
• serine-type D-Ala-D-Ala carboxypeptidase activity Source: EcoCycInferred from direct assayⁱ
  • Ref.12

    "The catalytic, glycosyl transferase and acyl transferase modules of the cell wall peptidoglycan-polymerizing penicillin-binding protein 1b of Escherichia coli."
    Terrak M., Ghosh T.K., van Heijenoort J., Van Beeumen J., Lampilas M., Aszodi J., Ayala J.A., Ghuysen J.-M., Nguyen-Disteche M.
    Mol. Microbiol. 34:350-364(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: ACTIVE SITE SER-510, MUTAGENESIS OF GLU-233; ASP-234 AND GLU-290.
  • "Lipid II: total synthesis of the bacterial cell wall precursor and utilization as a substrate for glycosyltransfer and transpeptidation by penicillin binding protein (PBP) 1b of Escherichia coli."
    Schwartz B., Markwalder J.A., Wang Y.
    J. Am. Chem. Soc. 123:11638-11643(2001) [PubMed] [Europe PMC] [Abstract]
  • "High-throughput screen for inhibitors of transglycosylase and/or transpeptidase activities of Escherichia coli penicillin binding protein 1b."
    Chandrakala B., Shandil R.K., Mehra U., Ravishankar S., Kaur P., Usha V., Joe B., deSousa S.M.
    Antimicrob. Agents Chemother. 48:30-40(2004) [PubMed] [Europe PMC] [Abstract]
  • "Screen for inhibitors of the coupled transglycosylase-transpeptidase of peptidoglycan biosynthesis in Escherichia coli."
    Ramachandran V., Chandrakala B., Kumar V.P., Usha V., Solapure S.M., de Sousa S.M.
    Antimicrob. Agents Chemother. 50:1425-1432(2006) [PubMed] [Europe PMC] [Abstract]
  • "Microplate assay for inhibitors of the transpeptidase activity of PBP1b of Escherichia coli."
    Jha R.K., de Sousa S.M.
    J Biomol Screen 11:1005-1014(2006) [PubMed] [Europe PMC] [Abstract]
  • "Activities and regulation of peptidoglycan synthases."
    Egan A.J., Biboy J., van't Veer I., Breukink E., Vollmer W.
    Philos. Trans. R. Soc. Lond., B, Biol. Sci. 370:0-0(2015) [PubMed] [Europe PMC] [Abstract]
  • Ref.6

    "Functional biosynthesis of cell wall peptidoglycan by polymorphic bifunctional polypeptides. Penicillin-binding protein 1Bs of Escherichia coli with activities of transglycosylase and transpeptidase."
    Nakagawa J., Tamaki S., Tomioka S., Matsuhashi M.
    J. Biol. Chem. 259:13937-13946(1984) [PubMed] [Europe PMC] [Abstract]

    Cited for: CATALYTIC ACTIVITY.

GO - Biological processⁱ

• cell wall organization Source: UniProtKB-KW
• peptidoglycan biosynthetic process Source: EcoCycInferred from direct assayⁱ
  • Ref.12

    "The catalytic, glycosyl transferase and acyl transferase modules of the cell wall peptidoglycan-polymerizing penicillin-binding protein 1b of Escherichia coli."
    Terrak M., Ghosh T.K., van Heijenoort J., Van Beeumen J., Lampilas M., Aszodi J., Ayala J.A., Ghuysen J.-M., Nguyen-Disteche M.
    Mol. Microbiol. 34:350-364(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: ACTIVE SITE SER-510, MUTAGENESIS OF GLU-233; ASP-234 AND GLU-290.
• positive regulation of bipolar cell growth Source: EcoliWikiInferred from direct assayⁱ
  • "Mutants of Escherichia coli which lack a component of penicillin-binding protein 1 are viable."
    Spratt B.G., Jobanputra V.
    FEBS Lett. 79:374-378(1977) [PubMed] [Europe PMC] [Abstract]
• regulation of cell shape Source: EcoCyc <p>Inferred from Genetic Interaction</p> <p>Used to describe "traditional" genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#igi">GO evidence code guide</a></p> Inferred from genetic interactionⁱ
  • "Unstable Escherichia coli L forms revisited: growth requires peptidoglycan synthesis."
    Joseleau-Petit D., Liebart J.C., Ayala J.A., D'Ari R.
    J. Bacteriol. 189:6512-6520(2007) [PubMed] [Europe PMC] [Abstract]
  • "Effects of furazlocillin, a beta-lactam antibiotic which binds selectively to penicillin-binding protein 3, on Escherichia coli mutants deficient in other penicillin-binding proteins."
    Schmidt L.S., Botta G., Park J.T.
    J. Bacteriol. 145:632-637(1981) [PubMed] [Europe PMC] [Abstract]
• response to antibiotic Source: EcoCycInferred from genetic interactionⁱ
  • "Unstable Escherichia coli L forms revisited: growth requires peptidoglycan synthesis."
    Joseleau-Petit D., Liebart J.C., Ayala J.A., D'Ari R.
    J. Bacteriol. 189:6512-6520(2007) [PubMed] [Europe PMC] [Abstract]
• response to X-ray Source: EcoCyc <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "Screen for genes involved in radiation survival of Escherichia coli and construction of a reference database."
    Sargentini N.J., Gularte N.P., Hudman D.A.
    Mutat. Res. 793:1-14(2016) [PubMed] [Europe PMC] [Abstract]

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

Topology

GO - Cellular componentⁱ

• integral component of plasma membrane Source: EcoCycInferred from direct assayⁱ
  • Ref.9

    "Use of a beta-lactamase fusion vector to investigate the organization of penicillin-binding protein 1B in the cytoplasmic membrane of Escherichia coli."
    Edelman A., Bowler L., Broome-Smith J.K., Spratt B.G.
    Mol. Microbiol. 1:101-106(1987) [PubMed] [Europe PMC] [Abstract]

    Cited for: TOPOLOGY.
• membrane Source: UniProtKBInferred from high throughput direct assayⁱ
  • "A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis."
    Lasserre J.P., Beyne E., Pyndiah S., Lapaillerie D., Claverol S., Bonneu M.
    Electrophoresis 27:3306-3321(2006) [PubMed] [Europe PMC] [Abstract]
• outer membrane-bounded periplasmic space Source: EcoCycInferred from direct assayⁱ
  • Ref.9

    "Use of a beta-lactamase fusion vector to investigate the organization of penicillin-binding protein 1B in the cytoplasmic membrane of Escherichia coli."
    Edelman A., Bowler L., Broome-Smith J.K., Spratt B.G.
    Mol. Microbiol. 1:101-106(1987) [PubMed] [Europe PMC] [Abstract]

    Cited for: TOPOLOGY.
• peptidoglycan-based cell wall Source: InterPro
• plasma membrane Source: EcoCycInferred from direct assayⁱ
  • "Localization of penicillin-binding protein 1b in Escherichia coli: immunoelectron microscopy and immunotransfer studies."
    Bayer M.H., Keck W., Bayer M.E.
    J. Bacteriol. 172:125-135(1990) [PubMed] [Europe PMC] [Abstract]

Keywords - Cellular componentⁱ

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

Mutagenesis

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Proteomic databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Region

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domainⁱ

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)ⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

        10         20         30         40         50
MAGNDREPIG RKGKPTRPVK QKVSRRRYED DDDYDDYDDY EDEEPMPRKG 
        60         70         80         90        100
KGKGKGRKPR GKRGWLWLLL KLAIVFAVLI AIYGVYLDQK IRSRIDGKVW 
       110        120        130        140        150
QLPAAVYGRM VNLEPDMTIS KNEMVKLLEA TQYRQVSKMT RPGEFTVQAN 
       160        170        180        190        200
SIEMIRRPFD FPDSKEGQVR ARLTFDGDHL ATIVNMENNR QFGFFRLDPR 
       210        220        230        240        250
LITMISSPNG EQRLFVPRSG FPDLLVDTLL ATEDRHFYEH DGISLYSIGR 
       260        270        280        290        300
AVLANLTAGR TVQGASTLTQ QLVKNLFLSS ERSYWRKANE AYMALIMDAR 
       310        320        330        340        350
YSKDRILELY MNEVYLGQSG DNEIRGFPLA SLYYFGRPVE ELSLDQQALL 
       360        370        380        390        400
VGMVKGASIY NPWRNPKLAL ERRNLVLRLL QQQQIIDQEL YDMLSARPLG 
       410        420        430        440        450
VQPRGGVISP QPAFMQLVRQ ELQAKLGDKV KDLSGVKIFT TFDSVAQDAA 
       460        470        480        490        500
EKAAVEGIPA LKKQRKLSDL ETAIVVVDRF SGEVRAMVGG SEPQFAGYNR 
       510        520        530        540        550
AMQARRSIGS LAKPATYLTA LSQPKIYRLN TWIADAPIAL RQPNGQVWSP 
       560        570        580        590        600
QNDDRRYSES GRVMLVDALT RSMNVPTVNL GMALGLPAVT ETWIKLGVPK 
       610        620        630        640        650
DQLHPVPAML LGALNLTPIE VAQAFQTIAS GGNRAPLSAL RSVIAEDGKV 
       660        670        680        690        700
LYQSFPQAER AVPAQAAYLT LWTMQQVVQR GTGRQLGAKY PNLHLAGKTG 
       710        720        730        740        750
TTNNNVDTWF AGIDGSTVTI TWVGRDNNQP TKLYGASGAM SIYQRYLANQ 
       760        770        780        790        800
TPTPLNLVPP EDIADMGVDY DGNFVCSGGM RILPVWTSDP QSLCQQSEMQ 
       810        820        830        840 
QQPSGNPFDQ SSQPQQQPQQ QPAQQEQKDS DGVAGWIKDM FGSN       

        10         20         30         40         50
MPRKGKGKGK GRKPRGKRGW LWLLLKLAIV FAVLIAIYGV YLDQKIRSRI 
        60         70         80         90        100
DGKVWQLPAA VYGRMVNLEP DMTISKNEMV KLLEATQYRQ VSKMTRPGEF 
       110        120        130        140        150
TVQANSIEMI RRPFDFPDSK EGQVRARLTF DGDHLATIVN MENNRQFGFF 
       160        170        180        190        200
RLDPRLITMI SSPNGEQRLF VPRSGFPDLL VDTLLATEDR HFYEHDGISL 
       210        220        230        240        250
YSIGRAVLAN LTAGRTVQGA STLTQQLVKN LFLSSERSYW RKANEAYMAL 
       260        270        280        290        300
IMDARYSKDR ILELYMNEVY LGQSGDNEIR GFPLASLYYF GRPVEELSLD 
       310        320        330        340        350
QQALLVGMVK GASIYNPWRN PKLALERRNL VLRLLQQQQI IDQELYDMLS 
       360        370        380        390        400
ARPLGVQPRG GVISPQPAFM QLVRQELQAK LGDKVKDLSG VKIFTTFDSV 
       410        420        430        440        450
AQDAAEKAAV EGIPALKKQR KLSDLETAIV VVDRFSGEVR AMVGGSEPQF 
       460        470        480        490        500
AGYNRAMQAR RSIGSLAKPA TYLTALSQPK IYRLNTWIAD APIALRQPNG 
       510        520        530        540        550
QVWSPQNDDR RYSESGRVML VDALTRSMNV PTVNLGMALG LPAVTETWIK 
       560        570        580        590        600
LGVPKDQLHP VPAMLLGALN LTPIEVAQAF QTIASGGNRA PLSALRSVIA 
       610        620        630        640        650
EDGKVLYQSF PQAERAVPAQ AAYLTLWTMQ QVVQRGTGRQ LGAKYPNLHL 
       660        670        680        690        700
AGKTGTTNNN VDTWFAGIDG STVTITWVGR DNNQPTKLYG ASGAMSIYQR 
       710        720        730        740        750
YLANQTPTPL NLVPPEDIAD MGVDYDGNFV CSGGMRILPV WTSDPQSLCQ 
       760        770        780        790 
QSEMQQQPSG NPFDQSSQPQ QQPQQQPAQQ EQKDSDGVAG WIKDMFGSN  

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautionⁱ

Experimental Info

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityⁱ

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 100% Identity
• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

Protein family/group databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ

Documents

1. SIMILARITY comments
   Index of protein domains and families
2. PATHWAY comments
   Index of metabolic and biosynthesis pathways
3. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references