D-alanyl-D-alanine dipeptidase

Details

Name
D-alanyl-D-alanine dipeptidase
Synonyms
  • 3.4.13.22
  • D-Ala-D-Ala dipeptidase
  • Vancomycin B-type resistance protein VanX
Gene Name
vanX
Organism
Enterococcus faecium
Amino acid sequence
>lcl|BSEQ0018832|D-alanyl-D-alanine dipeptidase
MEIGFTFLDEIVHGVRWDAKYATWDNFTGKPVDGYEVNRIVGTYELAESLLKAKELAATQ
GYGLLLWDGYRPKRAVNCFMQWAAQPENNLTKESYYPNIDRTEMISKGYVASKSSHSRGS
AIDLTLYRLDTGELVPMGSRFDFMDERSHHAANGISCNEAQNRRRLRSIMENSGFEAYSL
EWWHYVLRDEPYPNSYFDFPVK
Number of residues
202
Molecular Weight
23379.995
Theoretical pI
Not Available
GO Classification
Functions
dipeptidase activity / metallopeptidase activity / zinc ion binding
Processes
cell wall organization / response to antibiotic
Components
cell wall
General Function
Zinc ion binding
Specific Function
Catalyzes hydrolysis of the D-alanyl-D-alanine dipeptide.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0018833|D-alanyl-D-alanine dipeptidase (vanX)
ATGGAAATAGGATTTACTTTTTTAGATGAAATAGTACACGGTGTTCGTTGGGACGCTAAA
TATGCCACTTGGGATAATTTCACCGGAAAACCGGTTGACGGTTATGAAGTAAATCGCATT
GTAGGGACATACGAGTTGGCTGAATCGCTTTTGAAGGCAAAAGAACTGGCTGCTACCCAA
GGGTACGGATTGCTTCTATGGGACGGTTACCGTCCTAAGCGTGCTGTAAACTGTTTTATG
CAATGGGCTGCACAGCCGGAAAATAACCTGACAAAGGAAAGTTATTATCCCAATATTGAC
CGAACTGAGATGATTTCAAAAGGATACGTGGCTTCAAAATCAAGCCATAGCCGCGGCAGT
GCCATTGATCTTACGCTTTATCGATTAGACACGGGTGAGCTTGTACCAATGGGGAGCCGA
TTTGATTTTATGGATGAACGCTCTCATCATGCGGCAAATGGAATATCATGCAATGAAGCG
CAAAATCGCAGACGTTTGCGCTCCATCATGGAAAACAGTGGGTTTGAAGCATATAGCCTC
GAATGGTGGCACTATGTATTAAGAGACGAACCATACCCCAATAGCTATTTTGATTTCCCC
GTTAAATAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDQ06241
UniProtKB Entry NameVANX_ENTFC
General References
  1. Arthur M, Molinas C, Depardieu F, Courvalin P: Characterization of Tn1546, a Tn3-related transposon conferring glycopeptide resistance by synthesis of depsipeptide peptidoglycan precursors in Enterococcus faecium BM4147. J Bacteriol. 1993 Jan;175(1):117-27. [Article]
  2. Wu Z, Wright GD, Walsh CT: Overexpression, purification, and characterization of VanX, a D-, D-dipeptidase which is essential for vancomycin resistance in Enterococcus faecium BM4147. Biochemistry. 1995 Feb 28;34(8):2455-63. [Article]
  3. Arthur M, Molinas C, Courvalin P: The VanS-VanR two-component regulatory system controls synthesis of depsipeptide peptidoglycan precursors in Enterococcus faecium BM4147. J Bacteriol. 1992 Apr;174(8):2582-91. [Article]
  4. Reynolds PE, Depardieu F, Dutka-Malen S, Arthur M, Courvalin P: Glycopeptide resistance mediated by enterococcal transposon Tn1546 requires production of VanX for hydrolysis of D-alanyl-D-alanine. Mol Microbiol. 1994 Sep;13(6):1065-70. [Article]
  5. Bussiere DE, Pratt SD, Katz L, Severin JM, Holzman T, Park CH: The structure of VanX reveals a novel amino-dipeptidase involved in mediating transposon-based vancomycin resistance. Mol Cell. 1998 Jul;2(1):75-84. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails