Penicillin-binding protein 1B
Details
- Name
- Penicillin-binding protein 1B
- Synonyms
- Murein polymerase
- PBP-1b
- pbpF
- ponB
- Gene Name
- mrcB
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0000974|Penicillin-binding protein 1B MAGNDREPIGRKGKPTRPVKQKVSRRRYEDDDDYDDYDDYEDEEPMPRKGKGKGKGRKPR GKRGWLWLLLKLAIVFAVLIAIYGVYLDQKIRSRIDGKVWQLPAAVYGRMVNLEPDMTIS KNEMVKLLEATQYRQVSKMTRPGEFTVQANSIEMIRRPFDFPDSKEGQVRARLTFDGDHL ATIVNMENNRQFGFFRLDPRLITMISSPNGEQRLFVPRSGFPDLLVDTLLATEDRHFYEH DGISLYSIGRAVLANLTAGRTVQGASTLTQQLVKNLFLSSERSYWRKANEAYMALIMDAR YSKDRILELYMNEVYLGQSGDNEIRGFPLASLYYFGRPVEELSLDQQALLVGMVKGASIY NPWRNPKLALERRNLVLRLLQQQQIIDQELYDMLSARPLGVQPRGGVISPQPAFMQLVRQ ELQAKLGDKVKDLSGVKIFTTFDSVAQDAAEKAAVEGIPALKKQRKLSDLETAIVVVDRF SGEVRAMVGGSEPQFAGYNRAMQARRSIGSLAKPATYLTALSQPKIYRLNTWIADAPIAL RQPNGQVWSPQNDDRRYSESGRVMLVDALTRSMNVPTVNLGMALGLPAVTETWIKLGVPK DQLHPVPAMLLGALNLTPIEVAQAFQTIASGGNRAPLSALRSVIAEDGKVLYQSFPQAER AVPAQAAYLTLWTMQQVVQRGTGRQLGAKYPNLHLAGKTGTTNNNVDTWFAGIDGSTVTI TWVGRDNNQPTKLYGASGAMSIYQRYLANQTPTPLNLVPPEDIADMGVDYDGNFVCSGGM RILPVWTSDPQSLCQQSEMQQQPSGNPFDQSSQPQQQPQQQPAQQEQKDSDGVAGWIKDM FGSN
- Number of residues
- 844
- Molecular Weight
- 94291.875
- Theoretical pI
- 9.46
- GO Classification
- Functionsdrug binding / penicillin binding / peptidoglycan glycosyltransferase activity / serine-type D-Ala-D-Ala carboxypeptidase activityProcessescell wall organization / peptidoglycan biosynthetic process / proteolysis / regulation of cell shape / response to antibioticComponentsintegral component of external side of plasma membrane / membrane / peptidoglycan-based cell wall / plasma membrane
- General Function
- Serine-type d-ala-d-ala carboxypeptidase activity
- Specific Function
- Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits).
- Pfam Domain Function
- Transmembrane Regions
- 64-87
- Cellular Location
- Cell inner membrane
- Gene sequence
>lcl|BSEQ0018961|Penicillin-binding protein 1B (mrcB) ATGGCCGGGAATGACCGCGAGCCAATTGGACGCAAAGGGAAACCGACGCGTCCGGTCAAA CAAAAGGTAAGCCGTCGTCGTTACGAAGATGACGATGATTACGACGATTATGATGACTAT GAGGATGAAGAACCGATGCCGCGCAAAGGTAAGGGCAAAGGCAAAGGGCGTAAGCCTCGT GGCAAACGCGGCTGGCTATGGCTACTGCTAAAACTGGCTATCGTTTTTGCCGTGCTGATC GCCATTTACGGCGTTTATCTCGATCAAAAAATTCGTAGCCGTATTGATGGCAAGGTCTGG CAACTGCCTGCGGCAGTTTATGGCCGAATGGTCAATCTTGAGCCAGACATGACCATCAGC AAGAACGAGATGGTGAAGCTGCTGGAGGCGACCCAGTATCGTCAGGTGTCGAAAATGACC CGTCCTGGCGAATTTACCGTGCAGGCCAACAGCATTGAGATGATTCGCCGTCCGTTTGAT TTCCCGGACAGTAAAGAAGGACAGGTGCGCGCGCGTCTGACCTTTGATGGCGATCATCTG GCGACGATCGTCAATATGGAGAACAACCGTCAGTTCGGTTTCTTCCGTCTTGATCCGCGT CTGATCACCATGATCTCTTCGCCAAACGGTGAGCAGCGTCTGTTTGTGCCGCGCAGTGGT TTCCCGGATTTGCTGGTGGATACTTTGCTGGCGACAGAAGACCGTCATTTTTACGAGCAT GATGGAATCAGTCTCTACTCAATCGGACGTGCGGTGCTGGCAAACCTGACCGCCGGACGC ACGGTACAGGGTGCGAGTACGCTGACGCAACAGCTGGTGAAAAACCTGTTCCTCTCCAGC GAGCGTTCTTACTGGCGTAAAGCGAACGAAGCTTACATGGCGCTGATCATGGACGCGCGT TACAGCAAAGACCGTATTCTTGAGCTGTATATGAACGAGGTGTATCTCGGTCAGAGCGGC GACAACGAAATCCGCGGCTTCCCGCTGGCAAGCTTGTATTACTTTGGTCGCCCGGTAGAA GAGCTAAGCCTCGACCAGCAGGCGCTGTTAGTCGGTATGGTGAAAGGGGCGTCCATCTAC AACCCGTGGCGTAACCCAAAACTGGCGCTGGAGCGACGTAATCTGGTGCTGCGTCTGCTG CAACAGCAACAGATTATTGATCAAGAACTCTATGACATGTTGAGTGCCCGTCCGCTGGGG GTTCAGCCGCGCGGTGGGGTGATCTCTCCTCAGCCAGCCTTTATGCAACTGGTGCGTCAG GAGCTGCAGGCAAAACTGGGCGATAAGGTAAAAGATCTCTCCGGCGTGAAGATCTTCACT ACCTTTGACTCGGTGGCCCAGGACGCGGCAGAAAAAGCCGCCGTGGAAGGCATTCCGGCA CTGAAGAAACAGCGTAAGTTGAGCGATCTTGAAACTGCGATTGTGGTCGTCGACCGCTTT AGTGGTGAAGTTCGTGCGATGGTCGGAGGTTCTGAGCCGCAGTTTGCGGGCTACAACCGT GCGATGCAGGCGCGTCGTTCGATTGGTTCCCTTGCAAAACCAGCGACTTATCTGACGGCC TTAAGCCAGCCGAAAATCTATCGTCTGAATACGTGGATTGCGGATGCGCCAATTGCGCTG CGTCAGCCGAATGGCCAGGTCTGGTCACCGCAGAATGATGACCGTCGTTATAGCGAAAGC GGCAGAGTGATGCTGGTGGATGCGTTGACCCGTTCGATGAACGTGCCGACGGTAAATCTG GGGATGGCGCTGGGGCTGCCTGCGGTTACGGAGACCTGGATTAAACTGGGCGTACCGAAA GATCAGTTGCATCCGGTTCCGGCAATGCTGCTGGGGGCGTTGAACTTAACGCCAATCGAA GTGGCGCAGGCATTCCAGACCATCGCCAGCGGTGGTAACCGTGCACCGCTTTCTGCGCTG CGTTCGGTAATCGCGGAAGATGGCAAAGTGCTGTATCAGAGCTTCCCGCAGGCGGAACGC GCTGTTCCGGCGCAGGCGGCGTATCTGACACTATGGACCATGCAGCAGGTGGTACAACGC GGTACGGGTCGTCAGCTTGGGGCGAAATACCCGAACCTGCATCTGGCAGGGAAAACAGGG ACTACCAACAATAACGTAGATACCTGGTTTGCGGGCATTGACGGCAGCACGGTGACCATC ACCTGGGTCGGCCGTGATAACAACCAGCCGACCAAACTGTATGGTGCCAGCGGGGCAATG TCGATTTATCAGCGTTATCTGGCTAACCAGACGCCAACGCCGCTGAATCTTGTTCCGCCA GAAGATATTGCAGATATGGGCGTGGACTACGACGGCAACTTTGTTTGCAGCGGTGGCATG CGTATCTTGCCGGTCTGGACCAGCGATCCGCAATCGCTGTGCCAGCAGAGCGAGATGCAG CAGCAGCCGTCAGGCAATCCGTTTGATCAGTCTTCTCAGCCGCAGCAACAGCCGCAACAG CAACCTGCTCAGCAAGAGCAGAAAGACAGCGACGGTGTAGCCGGTTGGATCAAGGATATG TTTGGTAGTAATTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P02919 UniProtKB Entry Name PBPB_ECOLI GenBank Protein ID 42468 GenBank Gene ID X02163 - General References
- Broome-Smith JK, Edelman A, Yousif S, Spratt BG: The nucleotide sequences of the ponA and ponB genes encoding penicillin-binding protein 1A and 1B of Escherichia coli K12. Eur J Biochem. 1985 Mar 1;147(2):437-46. [Article]
- Fujita N, Mori H, Yura T, Ishihama A: Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region. Nucleic Acids Res. 1994 May 11;22(9):1637-9. [Article]
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
- Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
- Keck W, Glauner B, Schwarz U, Broome-Smith JK, Spratt BG: Sequences of the active-site peptides of three of the high-Mr penicillin-binding proteins of Escherichia coli K-12. Proc Natl Acad Sci U S A. 1985 Apr;82(7):1999-2003. [Article]
- Wang CC, Schultz DE, Nicholas RA: Localization of a putative second membrane association site in penicillin-binding protein 1B of Escherichia coli. Biochem J. 1996 May 15;316 ( Pt 1):149-56. [Article]
- Lefevre F, Remy MH, Masson JM: Topographical and functional investigation of Escherichia coli penicillin-binding protein 1b by alanine stretch scanning mutagenesis. J Bacteriol. 1997 Aug;179(15):4761-7. [Article]
- Edelman A, Bowler L, Broome-Smith JK, Spratt BG: Use of a beta-lactamase fusion vector to investigate the organization of penicillin-binding protein 1B in the cytoplasmic membrane of Escherichia coli. Mol Microbiol. 1987 Jul;1(1):101-6. [Article]
- Zijderveld CA, Aarsman ME, den Blaauwen T, Nanninga N: Penicillin-binding protein 1B of Escherichia coli exists in dimeric forms. J Bacteriol. 1991 Sep;173(18):5740-6. [Article]
- Vollmer W, von Rechenberg M, Holtje JV: Demonstration of molecular interactions between the murein polymerase PBP1B, the lytic transglycosylase MltA, and the scaffolding protein MipA of Escherichia coli. J Biol Chem. 1999 Mar 5;274(10):6726-34. [Article]
- Terrak M, Ghosh TK, van Heijenoort J, Van Beeumen J, Lampilas M, Aszodi J, Ayala JA, Ghuysen JM, Nguyen-Disteche M: The catalytic, glycosyl transferase and acyl transferase modules of the cell wall peptidoglycan-polymerizing penicillin-binding protein 1b of Escherichia coli. Mol Microbiol. 1999 Oct;34(2):350-64. [Article]
- Goffin C, Ghuysen JM: Multimodular penicillin-binding proteins: an enigmatic family of orthologs and paralogs. Microbiol Mol Biol Rev. 1998 Dec;62(4):1079-93. [Article]
- Sung MT, Lai YT, Huang CY, Chou LY, Shih HW, Cheng WC, Wong CH, Ma C: Crystal structure of the membrane-bound bifunctional transglycosylase PBP1b from Escherichia coli. Proc Natl Acad Sci U S A. 2009 Jun 2;106(22):8824-9. doi: 10.1073/pnas.0904030106. Epub 2009 May 19. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB01598 Imipenem approved yes inhibitor Details DB01329 Cefoperazone approved, investigational yes inhibitor Details DB01332 Ceftizoxime approved, withdrawn yes inhibitor Details DB01327 Cefazolin approved yes inhibitor Details DB01331 Cefoxitin approved yes inhibitor Details DB01328 Cefonicid approved, investigational yes inhibitor Details DB01415 Ceftibuten approved, investigational yes inhibitor Details DB00430 Cefpiramide approved yes inhibitor Details DB00438 Ceftazidime approved yes inhibitor Details DB00274 Cefmetazole approved, investigational yes inhibitor Details DB00303 Ertapenem approved, investigational yes inhibitor Details DB00689 Cephaloglycin approved yes antagonist Details DB01414 Cefacetrile experimental, vet_approved yes inhibitor Details DB04570 Latamoxef approved, investigational unknown inhibitor Details DB06211 Doripenem approved, investigational yes antagonistinhibitor Details DB11367 Cefroxadine withdrawn yes inhibitor Details DB01413 Cefepime approved, investigational yes inhibitor Details DB00578 Carbenicillin approved, investigational yes inhibitor Details DB09319 Carindacillin approved, investigational yes inhibitor Details DB09050 Ceftolozane approved, investigational unknown Details DB01602 Bacampicillin approved, investigational yes inhibitor Details DB01000 Cyclacillin approved yes inhibitor Details DB00671 Cefixime approved, investigational yes binder Details