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ENTFC:VANX

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Species (Taxon ID) Enterococcus faecium (Streptococcus faecium). (1352)
Gene Name(s) vanX
Protein Name(s) D-alanyl-D-alanine dipeptidase (ECO:0000255 with HAMAP-Rule:MF_01924)

D-Ala-D-Ala dipeptidase (ECO:0000255 with HAMAP-Rule:MF_01924) Vancomycin B-type resistance protein VanX

External Links
UniProt Q06241
EMBL M97297
PIR S72342
RefSeq YP_001019034.1
YP_001974795.1
YP_002128400.1
YP_009086374.1
YP_009090105.1
YP_976076.1
PDB 1R44
PDBsum 1R44
ProteinModelPortal Q06241
SMR Q06241
BindingDB Q06241
ChEMBL CHEMBL1681622
MEROPS M15.011
GeneID 4670250
4783136
6385878
6779646
BioCyc MetaCyc:MONOMER-15475
SABIO-RK Q06241
EvolutionaryTrace Q06241
GO GO:0005618
GO:0016805
GO:0046872
GO:0008237
GO:0071555
GO:0046677
Gene3D 3.30.1380.10
HAMAP MF_01924
InterPro IPR009045
IPR000755
Pfam PF01427
PIRSF PIRSF026671
SUPFAM SSF55166

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0010628

positive regulation of gene expression

PMID:8981985[1]

ECO:0000314

P

Fig. 4 shows production of VanX can be induced by different vancomycin concentrations. Expression of VanX is positively regulated in presence of vancomycin.

complete
CACAO 11321

Contributes to

GO:0016805

dipeptidase activity

PMID:9702193[2]

ECO:0000255

UniProtKB:Q06241


F

It is inferred that the protein VanX has dipeptidase properties based on it's similarities in structure to the known murine Sonic Hedgehog (an N-terminal fragment composing the hydrolytic functionality) and the D-ala-D-ala-carboxypeptidase S.Albus(composing the peptidase functionality). Fig 6A shows the alignment comparison of all three; VanX and MSH overlap for 92 alpha carbons, and VanX and S.Albus overlap for 114 alpha carbons. 6B shows at least 7 major homologous overlaps between VanX, MSH and S.Albus. In 6A, the superfamily relationship amongst VanX, MSH and S.Albus is validated by the similarities in active site location;in VanX it is located within residues 83-111, which aligns almost exact with MSH and S.Albus.

complete
CACAO 12640

involved_in

GO:0006508

proteolysis

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000755

P

Seeded From UniProt

complete

enables

GO:0008237

metallopeptidase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000755

F

Seeded From UniProt

complete

enables

GO:0016805

dipeptidase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000755

F

Seeded From UniProt

complete

enables

GO:0008270

zinc ion binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000161610

F

Seeded From UniProt

complete

enables

GO:0016805

dipeptidase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000161610

F

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0645

P

Seeded From UniProt

complete

involved_in

GO:0046677

response to antibiotic

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0046

P

Seeded From UniProt

complete

enables

GO:0008233

peptidase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0645

F

Seeded From UniProt

complete

involved_in

GO:0071555

cell wall organization

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0961

P

Seeded From UniProt

complete

enables

GO:0008237

metallopeptidase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0482

F

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

enables

GO:0016805

dipeptidase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0224

F

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. Arthur, M et al. (1997) The VanS sensor negatively controls VanR-mediated transcriptional activation of glycopeptide resistance genes of Tn1546 and related elements in the absence of induction. J. Bacteriol. 179 97-106 PubMed GONUTS page
  2. Bussiere, DE et al. (1998) The structure of VanX reveals a novel amino-dipeptidase involved in mediating transposon-based vancomycin resistance. Mol. Cell 2 75-84 PubMed GONUTS page