D-alanyl-D-alanine carboxypeptidase DacC
Details
- Name
- D-alanyl-D-alanine carboxypeptidase DacC
- Synonyms
- 3.4.16.4
- DD-carboxypeptidase
- PBP-6
- Penicillin-binding protein 6
- Gene Name
- dacC
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0012564|D-alanyl-D-alanine carboxypeptidase DacC MTQYSSLLRGLAAGSAFLFLFAPTAFAAEQTVEAPSVDARAWILMDYASGKVLAEGNADE KLDPASLTKIMTSYVVGQALKADKIKLTDMVTVGKDAWATGNPALRGSSVMFLKPGDQVS VADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYAKKLGLTNTTFQTVHGLDAPGQ FSTARDMALLGKALIHDVPEEYAIHKEKEFTFNKIRQPNRNRLLWSSNLNVDGMKTGTTA GAGYNLVASATQGDMRLISVVLGAKTDRIRFNESEKLLTWGFRFFETVTPIKPDATFVTQ RVWFGDKSEVNLGAGEAGSVTIPRGQLKNLKASYTLTEPQLTAPLKKGQVVGTIDFQLNG KSIEQRPLIVMENVEEGGFFGRVWDFVMMKFHQWFGSWFS
- Number of residues
- 400
- Molecular Weight
- 43608.595
- Theoretical pI
- 8.38
- GO Classification
- Functionscarboxypeptidase activity / endopeptidase activity / penicillin binding / serine-type D-Ala-D-Ala carboxypeptidase activityProcessescell wall organization / peptidoglycan biosynthetic process / regulation of cell shape / response to drugComponentsintegral component of plasma membrane
- General Function
- Serine-type d-ala-d-ala carboxypeptidase activity
- Specific Function
- Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors.
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Cell inner membrane
- Gene sequence
>lcl|BSEQ0012565|D-alanyl-D-alanine carboxypeptidase DacC (dacC) ATGACGCAATACTCCTCTCTCCTTCGTGGTCTTGCAGCGGGTTCTGCATTTTTATTCCTT TTTGCCCCAACGGCATTCGCGGCGGAACAAACCGTTGAAGCGCCGAGCGTGGATGCGCGT GCATGGATTTTAATGGATTACGCCAGCGGTAAAGTGCTGGCAGAAGGCAATGCGGATGAG AAACTGGATCCCGCGAGCCTGACTAAAATCATGACCAGCTATGTGGTTGGGCAGGCGCTT AAGGCCGATAAGATTAAACTCACCGATATGGTGACGGTCGGTAAAGATGCCTGGGCGACG GGAAATCCGGCACTGCGTGGTTCATCGGTAATGTTCCTCAAACCGGGCGATCAGGTTTCG GTGGCAGACTTGAACAAAGGTGTGATTATCCAGTCCGGTAATGACGCCTGTATTGCGCTG GCTGATTACGTTGCCGGGAGCCAGGAGTCATTTATTGGTCTGATGAATGGTTATGCCAAA AAACTGGGTCTGACCAACACTACCTTCCAGACGGTGCACGGCCTGGATGCGCCGGGGCAG TTCAGCACCGCGCGCGATATGGCATTGCTGGGTAAAGCATTGATCCACGATGTGCCGGAA GAGTACGCCATTCATAAAGAGAAAGAGTTCACCTTCAACAAAATTCGTCAGCCTAACCGT AACCGTCTGCTGTGGAGCAGCAATCTGAATGTTGATGGCATGAAGACAGGAACCACGGCA GGCGCGGGATATAATCTGGTTGCTTCGGCTACCCAGGGCGATATGCGTTTAATCTCCGTA GTGTTGGGGGCGAAAACCGACCGTATCCGTTTTAATGAGTCTGAGAAATTATTGACCTGG GGTTTCCGCTTCTTTGAAACCGTGACGCCAATTAAACCTGATGCCACCTTTGTGACTCAG CGCGTCTGGTTTGGTGATAAGAGCGAAGTGAATCTCGGGGCAGGTGAAGCGGGCTCAGTG ACCATACCGCGTGGGCAGCTGAAAAACCTGAAAGCGAGTTATACGTTAACGGAACCGCAG CTTACCGCACCGCTGAAAAAAGGTCAGGTTGTCGGGACCATTGATTTCCAGCTTAACGGT AAATCCATTGAGCAGCGTCCGCTGATCGTGATGGAAAATGTGGAAGAGGGCGGATTCTTT GGTCGGGTGTGGGATTTCGTGATGATGAAATTCCATCAGTGGTTCGGCAGCTGGTTCTCT TAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P08506 UniProtKB Entry Name DACC_ECOLI GenBank Protein ID 41218 GenBank Gene ID X06480 - General References
- Broome-Smith JK, Ioannidis I, Edelman A, Spratt BG: Nucleotide sequences of the penicillin-binding protein 5 and 6 genes of Escherichia coli. Nucleic Acids Res. 1988 Feb 25;16(4):1617. [Article]
- Oshima T, Aiba H, Baba T, Fujita K, Hayashi K, Honjo A, Ikemoto K, Inada T, Itoh T, Kajihara M, Kanai K, Kashimoto K, Kimura S, Kitagawa M, Makino K, Masuda S, Miki T, Mizobuchi K, Mori H, Motomura K, Nakamura Y, Nashimoto H, Nishio Y, Saito N, Horiuchi T, et al.: A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map. DNA Res. 1996 Jun 30;3(3):137-55. [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]
- Waxman DJ, Amanuma H, Strominger JL: Amino acid sequence homologies between Escherichia coli penicillin-binding protein 5 and class A beta-lactamases. FEBS Lett. 1982 Mar 22;139(2):159-63. [Article]
- Jackson ME, Pratt JM: An 18 amino acid amphiphilic helix forms the membrane-anchoring domain of the Escherichia coli penicillin-binding protein 5. Mol Microbiol. 1987 Jul;1(1):23-8. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB01329 Cefoperazone approved, investigational yes inhibitor Details DB01331 Cefoxitin approved yes inhibitor Details DB00430 Cefpiramide approved yes inhibitor Details DB00274 Cefmetazole approved, investigational yes inhibitor Details DB00303 Ertapenem approved, investigational yes inhibitor Details DB01332 Ceftizoxime approved, withdrawn unknown binder 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