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
- Functionscarboxypeptidase activity / endopeptidase activity / penicillin binding / serine-type D-Ala-D-Ala carboxypeptidase activityProcessescell 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 antibioticComponentsouter 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
- Peptidase_S13 (PF02113)
- 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
Resource Link UniProtKB ID P24228 UniProtKB Entry Name DACB_ECOLI GenBank Protein ID 41216 GenBank Gene ID X59460 - General References
- 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. [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]
- 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. [Article]
- 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. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB00760 Meropenem approved, investigational yes inhibitor Details DB01329 Cefoperazone approved, investigational yes inhibitor Details DB01331 Cefoxitin approved yes inhibitor Details DB01328 Cefonicid approved, investigational yes inhibitor Details DB00303 Ertapenem approved, investigational yes inhibitor Details DB04570 Latamoxef approved, investigational unknown inhibitor Details DB00417 Phenoxymethylpenicillin approved, vet_approved unknown Details DB14879 Cefiderocol 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