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
Functions
beta-lactamase activity / carboxypeptidase activity / endopeptidase activity / penicillin binding / serine-type D-Ala-D-Ala carboxypeptidase activity
Processes
cell wall macromolecule metabolic process / cell wall organization / peptidoglycan biosynthetic process / peptidoglycan metabolic process / regulation of cell shape
Components
integral 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
ResourceLink
UniProtKB IDP0AEB2
UniProtKB Entry NameDACA_ECOLI
GenBank Gene IDX06479
General References
  1. 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. [PubMed:3279397]
  2. 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. [PubMed:8905232]
  3. 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]
  4. 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]
  5. 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. [PubMed:6319180]
  6. 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. [PubMed:3316191]
  7. 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. [PubMed:7042389]
  8. 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. [PubMed:1597468]
  9. 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. [PubMed:8424800]
  10. 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. [PubMed:9298644]
  11. 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. [PubMed:10967102]
  12. 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. [PubMed:14555648]
  13. 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. [PubMed:15938610]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB04647BOC-GAMMA-D-GLU-L-LYS(CBZ)-D-BOROALAexperimentalunknownDetails
DB01329Cefoperazoneapproved, investigationalyesinhibitorDetails
DB01331CefoxitinapprovedyesinhibitorDetails
DB00274Cefmetazoleapproved, investigationalyesinhibitorDetails
DB00578Carbenicillinapproved, investigationalyesinhibitorDetails
DB09319Carindacillinapproved, investigationalyesinhibitorDetails
DB09050Ceftolozaneapproved, investigationalunknownDetails