D-alanyl-D-alanine endopeptidase

Details

Name
D-alanyl-D-alanine endopeptidase
Synonyms
  • 3.4.21.-
  • DD-endopeptidase
  • PBP-7
  • Penicillin-binding protein 7
  • yohB
Gene Name
pbpG
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0009351|D-alanyl-D-alanine endopeptidase
MPKFRVSLFSLALMLAVPFAPQAVAKTAAATTASQPEIASGSAMIVDLNTNKVIYSNHPD
LVRPIASISKLMTAMVVLDARLPLDEKLKVDISQTPEMKGVYSRVRLNSEISRKDMLLLA
LMSSENRAAASLAHHYPGGYKAFIKAMNAKAKSLGMNNTRFVEPTGLSVHNVSTARDLTK
LLIASKQYPLIGQLSTTREDMATFSNPTYTLPFRNTNHLVYRDNWNIQLTKTGFTNAAGH
CLVMRTVINNKPVALVVMDAFGKYTHFADASRLRTWIETGKVMPVPAAALSYKKQKAAQM
AAAGQTAQND
Number of residues
310
Molecular Weight
33887.085
Theoretical pI
Not Available
GO Classification
Functions
endopeptidase activity / serine-type D-Ala-D-Ala carboxypeptidase activity
Processes
cell wall organization / FtsZ-dependent cytokinesis / peptidoglycan biosynthetic process / peptidoglycan metabolic process / regulation of cell shape / response to drug
Components
integral component of plasma membrane / periplasmic space
General Function
Serine-type d-ala-d-ala carboxypeptidase activity
Specific Function
Cell wall formation. May play a specialized role in remodeling the cell wall. Specifically hydrolyzes the DD-diaminopimelate-alanine bonds in high-molecular-mass murein sacculi.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Periplasm
Gene sequence
>lcl|BSEQ0013105|D-alanyl-D-alanine endopeptidase (pbpG)
ATGCCGAAATTTCGAGTTTCTTTATTTAGCCTGGCCCTGATGCTGGCTGTGCCTTTTGCA
CCGCAGGCCGTTGCGAAAACGGCAGCCGCTACCACCGCTTCACAACCGGAAATTGCCTCC
GGTAGCGCGATGATTGTTGATCTGAATACCAACAAAGTGATCTATTCGAACCACCCGGAT
CTGGTGCGTCCGATTGCGTCTATCAGCAAATTAATGACCGCGATGGTTGTGCTGGATGCA
CGACTGCCGCTGGATGAAAAACTAAAAGTGGATATCAGCCAGACGCCGGAGATGAAAGGG
GTCTATTCGCGCGTACGACTGAATAGCGAAATCAGCCGTAAAGATATGCTGTTGCTGGCG
CTGATGTCTTCAGAAAACCGCGCGGCGGCAAGCCTTGCGCACCATTATCCCGGTGGTTAC
AAAGCCTTTATTAAGGCAATGAATGCGAAAGCGAAATCGCTCGGAATGAACAACACGCGC
TTTGTTGAACCTACCGGATTGTCGGTGCATAACGTTTCAACTGCCCGTGACTTAACCAAA
CTGCTCATTGCCAGCAAACAATATCCGTTGATCGGGCAGTTAAGTACTACCCGGGAAGAT
ATGGCAACCTTCTCTAATCCGACGTATACGCTGCCGTTCCGCAATACTAATCATCTGGTG
TATCGCGATAACTGGAATATTCAGTTAACCAAAACCGGCTTTACCAATGCGGCGGGCCAT
TGTCTGGTGATGCGTACGGTTATCAATAATAAACCGGTGGCGCTGGTAGTGATGGACGCG
TTTGGCAAATATACCCATTTTGCCGATGCCAGCCGCCTGCGTACCTGGATTGAAACCGGT
AAAGTGATGCCTGTGCCGGCAGCAGCGTTGAGCTATAAAAAACAAAAAGCCGCCCAAATG
GCGGCGGCGGGGCAGACGGCACAGAACGATTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP0AFI5
UniProtKB Entry NamePBP7_ECOLI
General References
  1. 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]
  2. 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]
  3. Campbell HD, Rogers BL, Young IG: Nucleotide sequence of the respiratory D-lactate dehydrogenase gene of Escherichia coli. Eur J Biochem. 1984 Oct 15;144(2):367-73. [Article]
  4. Henderson TA, Templin M, Young KD: Identification and cloning of the gene encoding penicillin-binding protein 7 of Escherichia coli. J Bacteriol. 1995 Apr;177(8):2074-9. [Article]
  5. Romeis T, Holtje JV: Penicillin-binding protein 7/8 of Escherichia coli is a DD-endopeptidase. Eur J Biochem. 1994 Sep 1;224(2):597-604. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01331CefoxitinapprovedyesinhibitorDetails