D-alanyl-D-alanine carboxypeptidase DacA
Details
- Name
- D-alanyl-D-alanine carboxypeptidase DacA
- Synonyms
- 3.4.16.4
- Beta-lactamase
- DD-carboxypeptidase
- PBP-5
- Penicillin-binding protein 5
- pfv
- Gene Name
- dacA
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0004061|D-alanyl-D-alanine carboxypeptidase DacA MNTIFSARIMKRLALTTALCTAFISAAHADDLNIKTMIPGVPQIDAESYILIDYNSGKVL AEQNADVRRDPASLTKMMTSYVIGQAMKAGKFKETDLVTIGNDAWATGNPVFKGSSLMFL KPGMQVPVSQLIRGINLQSGNDACVAMADFAAGSQDAFVGLMNSYVNALGLKNTHFQTVH GLDADGQYSSARDMALIGQALIRDVPNEYSIYKEKEFTFNGIRQLNRNGLLWDNSLNVDG IKTGHTDKAGYNLVASATEGQMRLISAVMGGRTFKGREAESKKLLTWGFRFFETVNPLKV GKEFASEPVWFGDSDRASLGVDKDVYLTIPRGRMKDLKASYVLNSSELHAPLQKNQVVGT INFQLDGKTIEQRPLVVLQEIPEGNFFGKIIDYIKLMFHHWFG
- Number of residues
- 403
- Molecular Weight
- 44443.62
- Theoretical pI
- 8.58
- GO Classification
- Functionsbeta-lactamase activity / carboxypeptidase activity / endopeptidase activity / penicillin binding / serine-type D-Ala-D-Ala carboxypeptidase activityProcessescell wall macromolecule metabolic process / cell wall organization / peptidoglycan biosynthetic process / peptidoglycan metabolic process / regulation of cell shapeComponentsintegral 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|BSEQ0020585|D-alanyl-D-alanine carboxypeptidase DacA (dacA) ATGAATACCATTTTTTCCGCTCGTATCATGAAGCGCCTGGCGCTCACCACGGCTCTTTGC ACAGCCTTTATCTCTGCTGCACATGCCGATGACCTGAATATCAAAACTATGATCCCGGGT GTACCGCAGATCGATGCGGAGTCCTACATCCTGATTGACTATAACTCCGGCAAAGTGCTC GCCGAACAGAACGCAGATGTCCGCCGCGATCCTGCCAGCCTGACCAAAATGATGACCAGT TACGTTATCGGCCAGGCAATGAAAGCCGGTAAATTTAAAGAAACTGATTTAGTCACTATC GGCAACGACGCATGGGCCACCGGTAACCCGGTGTTTAAAGGTTCTTCGCTGATGTTCCTC AAACCGGGCATGCAGGTTCCGGTTTCTCAGCTGATCCGCGGTATTAACCTGCAATCGGGT AACGATGCTTGTGTCGCCATGGCCGATTTTGCCGCTGGTAGCCAGGACGCTTTTGTTGGC TTGATGAACAGCTACGTTAACGCACTGGGCCTGAAAAATACCCACTTCCAGACGGTACAT GGTCTGGATGCTGATGGTCAGTACAGCTCCGCGCGAGATATGGCGCTGATCGGCCAGGCA TTGATCCGTGACGTACCGAATGAATACTCGATCTATAAAGAAAAAGAATTTACGTTTAAC GGTATTCGCCAGCTGAACCGTAACGGCCTGTTATGGGATAACAGCCTGAATGTCGACGGC ATCAAAACCGGACACACTGACAAAGCAGGTTACAACCTTGTTGCTTCTGCGACTGAAGGC CAGATGCGCTTGATTTCTGCGGTAATGGGCGGACGTACTTTTAAAGGCCGTGAAGCCGAA AGTAAAAAACTGCTAACCTGGGGCTTCCGTTTCTTTGAAACCGTTAACCCACTGAAAGTA GGTAAAGAGTTCGCCTCTGAACCGGTTTGGTTTGGTGATTCTGATCGCGCTTCGTTAGGG GTTGATAAAGACGTGTACCTGACCATTCCGCGTGGTCGCATGAAAGATCTGAAAGCCAGC TATGTGCTGAACAGCAGTGAATTGCATGCGCCGCTGCAAAAGAATCAGGTCGTCGGAACT ATCAACTTCCAGCTTGATGGCAAAACGATCGAGCAACGCCCGCTGGTTGTGTTGCAAGAA ATCCCGGAAGGTAACTTCTTCGGCAAAATCATTGATTACATTAAATTAATGTTCCATCAC TGGTTTGGTTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P0AEB2 UniProtKB Entry Name DACA_ECOLI GenBank Gene ID X06479 - 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]
- Broome-Smith J, Spratt BG: An amino acid substitution that blocks the deacylation step in the enzyme mechanism of penicillin-binding protein 5 of Escherichia coli. FEBS Lett. 1984 Jan 9;165(2):185-9. [Article]
- Takase I, Ishino F, Wachi M, Kamata H, Doi M, Asoh S, Matsuzawa H, Ohta T, Matsuhashi M: Genes encoding two lipoproteins in the leuS-dacA region of the Escherichia coli chromosome. J Bacteriol. 1987 Dec;169(12):5692-9. [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]
- Malhotra KT, Nicholas RA: Substitution of lysine 213 with arginine in penicillin-binding protein 5 of Escherichia coli abolishes D-alanine carboxypeptidase activity without affecting penicillin binding. J Biol Chem. 1992 Jun 5;267(16):11386-91. [Article]
- van der Linden MP, de Haan L, Keck W: Domain organization of penicillin-binding protein 5 from Escherichia coli analysed by C-terminal truncation. Biochem J. 1993 Jan 15;289 ( Pt 2):593-8. [Article]
- VanBogelen RA, Abshire KZ, Moldover B, Olson ER, Neidhardt FC: Escherichia coli proteome analysis using the gene-protein database. Electrophoresis. 1997 Aug;18(8):1243-51. [Article]
- Davies C, White SW, Nicholas RA: Crystal structure of a deacylation-defective mutant of penicillin-binding protein 5 at 2.3-A resolution. J Biol Chem. 2001 Jan 5;276(1):616-23. [Article]
- Nicholas RA, Krings S, Tomberg J, Nicola G, Davies C: Crystal structure of wild-type penicillin-binding protein 5 from Escherichia coli: implications for deacylation of the acyl-enzyme complex. J Biol Chem. 2003 Dec 26;278(52):52826-33. Epub 2003 Oct 10. [Article]
- Nicola G, Peddi S, Stefanova M, Nicholas RA, Gutheil WG, Davies C: Crystal structure of Escherichia coli penicillin-binding protein 5 bound to a tripeptide boronic acid inhibitor: a role for Ser-110 in deacylation. Biochemistry. 2005 Jun 14;44(23):8207-17. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB04647 BOC-GAMMA-D-GLU-L-LYS(CBZ)-D-BOROALA experimental unknown Details DB01329 Cefoperazone approved, investigational yes inhibitor Details DB01331 Cefoxitin approved yes inhibitor Details DB00274 Cefmetazole approved, investigational yes inhibitor Details DB01147 Cloxacillin approved, investigational, vet_approved 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 DB00671 Cefixime approved, investigational yes binder Details