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
Functions
drug binding / penicillin binding / peptidoglycan glycosyltransferase activity / serine-type D-Ala-D-Ala carboxypeptidase activity
Processes
cell wall organization / peptidoglycan biosynthetic process / proteolysis / regulation of cell shape / response to antibiotic
Components
integral 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
ResourceLink
UniProtKB IDP02919
UniProtKB Entry NamePBPB_ECOLI
GenBank Protein ID42468
GenBank Gene IDX02163
General References
  1. 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. [PubMed:3882429]
  2. 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. [PubMed:8202364]
  3. 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. [PubMed:9278503]
  4. 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. [PubMed:16738553]
  5. 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. [PubMed:3920658]
  6. 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. [PubMed:8645198]
  7. 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. [PubMed:9244263]
  8. 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. [PubMed:3330753]
  9. 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. [PubMed:1885547]
  10. 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. [PubMed:10037771]
  11. 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. [PubMed:10564478]
  12. 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. [PubMed:9841666]
  13. 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. [PubMed:19458048]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01598ImipenemapprovedyesinhibitorDetails
DB01329Cefoperazoneapproved, investigationalyesinhibitorDetails
DB01332Ceftizoximeapproved, investigationalyesinhibitorDetails
DB01327CefazolinapprovedyesinhibitorDetails
DB01331CefoxitinapprovedyesinhibitorDetails
DB01328Cefonicidapproved, investigationalyesinhibitorDetails
DB01415Ceftibutenapproved, investigationalyesinhibitorDetails
DB00430CefpiramideapprovedyesinhibitorDetails
DB00438CeftazidimeapprovedyesinhibitorDetails
DB00274Cefmetazoleapproved, investigationalyesinhibitorDetails
DB00303Ertapenemapproved, investigationalyesinhibitorDetails
DB01414Cefacetrileexperimental, vet_approvedyesinhibitorDetails
DB04570Latamoxefapproved, investigationalunknowninhibitorDetails
DB06211Doripenemapproved, investigationalyesantagonistinhibitorDetails
DB11367CefroxadinewithdrawnyesinhibitorDetails
DB00578Carbenicillinapproved, investigationalyesinhibitorDetails
DB09319Carindacillinapproved, investigationalyesinhibitorDetails
DB09050Ceftolozaneapproved, investigationalunknownDetails