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
- Functionsdipeptidase activity / metallopeptidase activity / zinc ion bindingProcessescell wall organization / response to antibioticComponentscell wall
- General Function
- Zinc ion binding
- Specific Function
- Catalyzes hydrolysis of the D-alanyl-D-alanine dipeptide.
- Pfam Domain Function
- Peptidase_M15 (PF01427)
- 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
Resource Link UniProtKB ID Q06241 UniProtKB Entry Name VANX_ENTFC - General References
- 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]
- 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]
- 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]
- 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]
- 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 ID Name Drug group Pharmacological action? Actions Details