D-alanyl-D-alanine carboxypeptidase DacB

Details

Name
D-alanyl-D-alanine carboxypeptidase DacB
Synonyms
  • 3.4.16.4
  • D-alanyl-D-alanine endopeptidase
  • DD-carboxypeptidase
  • DD-endopeptidase
  • PBP-4
  • Penicillin-binding protein 4
Gene Name
dacB
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0019003|D-alanyl-D-alanine carboxypeptidase DacB
MRFSRFIIGLTSCIAFSVQAANVDEYITQLPAGANLALMVQKVGASAPAIDYHSQQMALP
ASTQKVITALAALIQLGPDFRFTTTLETKGNVENGVLKGDLVARFGADPTLKRQDIRNMV
ATLKKSGVNQIDGNVLIDTSIFASHDKAPGWPWNDMTQCFSAPPAAAIVDRNCFSVSLYS
APKPGDMAFIRVASYYPVTMFSQVRTLPRGSAEAQYCELDVVPGDLNRFTLTGCLPQRSE
PLPLAFAVQDGASYAGAILKDELKQAGITWSGTLLRQTQVNEPGTVVASKQSAPLHDLLK
IMLKKSDNMIADTVFRMIGHARFNVPGTWRAGSDAVRQILRQQAGVDIGNTIIADGSGLS
RHNLIAPATMMQVLQYIAQHDNELNFISMLPLAGYDGSLQYRAGLHQAGVDGKVSAKTGS
LQGVYNLAGFITTASGQRMAFVQYLSGYAVEPADQRNRRIPLVRFESRLYKDIYQNN
Number of residues
477
Molecular Weight
51797.85
Theoretical pI
9.02
GO Classification
Functions
carboxypeptidase activity / endopeptidase activity / penicillin binding / serine-type D-Ala-D-Ala carboxypeptidase activity
Processes
cell wall macromolecule catabolic process / cell wall organization / FtsZ-dependent cytokinesis / peptidoglycan biosynthetic process / peptidoglycan catabolic process / peptidoglycan metabolic process / peptidoglycan turnover / regulation of cell shape / response to antibiotic
Components
outer membrane-bounded periplasmic space
General Function
Serine-type d-ala-d-ala carboxypeptidase activity
Specific Function
Not involved in transpeptidation but exclusively catalyzes a DD-carboxypeptidase and DD-endopeptidase reaction.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Periplasm
Gene sequence
>lcl|BSEQ0019004|D-alanyl-D-alanine carboxypeptidase DacB (dacB)
ATGCGATTTTCCAGATTTATCATCGGATTGACCAGCTGTATAGCGTTCAGTGTTCAGGCC
GCAAATGTTGATGAGTACATTACTCAACTCCCCGCTGGTGCCAACCTTGCCCTGATGGTG
CAAAAAGTCGGCGCGTCGGCCCCCGCTATTGATTACCACAGTCAGCAGATGGCGCTGCCT
GCCAGTACCCAGAAAGTGATTACTGCGCTGGCGGCGTTGATTCAACTCGGCCCCGATTTT
CGTTTTACCACGACGCTTGAAACCAAAGGCAATGTGGAAAACGGCGTACTTAAGGGTGAC
TTAGTGGCGCGATTTGGTGCCGATCCGACGTTAAAACGTCAGGATATTCGCAATATGGTC
GCGACTTTGAAAAAATCTGGCGTCAACCAAATCGATGGCAATGTGTTGATAGATACCTCC
ATTTTCGCCAGCCACGATAAAGCCCCCGGCTGGCCATGGAATGACATGACACAATGCTTT
AGCGCTCCGCCTGCCGCCGCCATAGTTGACCGCAACTGTTTCTCCGTCTCGCTCTACAGT
GCCCCAAAGCCTGGTGATATGGCTTTTATACGCGTGGCATCTTATTACCCCGTTACGATG
TTCAGCCAGGTACGCACCCTCCCCCGTGGTTCTGCCGAAGCGCAATACTGCGAACTGGAT
GTGGTGCCAGGCGACCTGAACCGCTTTACGCTGACGGGATGCCTGCCACAACGTTCTGAG
CCGCTCCCGTTGGCTTTTGCCGTGCAGGATGGAGCCAGCTATGCCGGTGCAATTCTGAAA
GATGAGTTAAAACAGGCGGGTATCACCTGGAGCGGAACACTGCTGCGCCAGACTCAGGTT
AACGAACCTGGAACGGTAGTTGCCAGTAAACAGTCGGCCCCGCTGCACGATCTGCTTAAG
ATTATGCTGAAAAAGTCGGACAACATGATCGCCGATACGGTTTTCCGCATGATAGGCCAT
GCGCGCTTCAATGTGCCTGGAACATGGCGGGCCGGGTCGGACGCCGTGCGTCAGATCCTG
CGCCAGCAAGCCGGTGTCGATATTGGAAACACCATTATTGCCGATGGTTCAGGGCTTTCG
CGGCATAACCTGATTGCCCCCGCCACCATGATGCAGGTGCTGCAATACATTGCCCAACAC
GACAATGAACTTAACTTTATCTCCATGCTGCCGCTGGCGGGCTATGACGGCTCTTTGCAG
TACCGTGCAGGTCTGCATCAGGCGGGCGTGGATGGAAAAGTCTCAGCGAAAACCGGTTCG
TTGCAGGGGGTATATAACCTGGCGGGATTCATTACCACAGCGAGCGGGCAACGAATGGCG
TTTGTGCAATATCTTTCTGGCTATGCAGTAGAACCTGCGGATCAGCGTAATCGCCGTATT
CCGTTAGTGCGTTTTGAAAGCCGTTTGTATAAAGATATTTATCAGAACAATTAG
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP24228
UniProtKB Entry NameDACB_ECOLI
GenBank Protein ID41216
GenBank Gene IDX59460
General References
  1. Mottl H, Terpstra P, Keck W: Penicillin-binding protein 4 of Escherichia coli shows a novel type of primary structure among penicillin-interacting proteins. FEMS Microbiol Lett. 1991 Mar 1;62(2-3):213-20. [PubMed:2040429]
  2. 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]
  3. 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]
  4. Kishida H, Unzai S, Roper DI, Lloyd A, Park SY, Tame JR: Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli, both in the native form and covalently linked to various antibiotics. Biochemistry. 2006 Jan 24;45(3):783-92. [PubMed:16411754]
  5. Korat B, Mottl H, Keck W: Penicillin-binding protein 4 of Escherichia coli: molecular cloning of the dacB gene, controlled overexpression, and alterations in murein composition. Mol Microbiol. 1991 Mar;5(3):675-84. [PubMed:2046551]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00760Meropenemapproved, investigationalyesinhibitorDetails
DB01329Cefoperazoneapproved, investigationalyesinhibitorDetails
DB01331CefoxitinapprovedyesinhibitorDetails
DB01328Cefonicidapproved, investigationalyesinhibitorDetails
DB00303Ertapenemapproved, investigationalyesinhibitorDetails
DB04570Latamoxefapproved, investigationalunknowninhibitorDetails
DB00417Phenoxymethylpenicillinapproved, vet_approvedunknownDetails
DB00578Carbenicillinapproved, investigationalyesinhibitorDetails
DB09319Carindacillinapproved, investigationalyesinhibitorDetails
DB09050Ceftolozaneapproved, investigationalunknownDetails