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UniProt functional annotation for Q47746 | ||
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| UniProt code: Q47746. |
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| Organism: | |
Enterococcus faecalis (strain ATCC 700802 / V583). |
| Taxonomy: | |
Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; Enterococcus. |
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| Function: | |
Carboxypeptidase that cleaves the C-terminal D-alanine residue from the peptidoglycan-derived pentapeptide L-Ala-gamma-D-Glu- L-Lys-D-Ala-D-Ala in vitro. Therefore, should contribute in vivo to the hydrolysis of the D-alanyl-D-alanine-containing peptidoglycan precursors. May increase the level of glycopeptide antibiotics resistance by decreasing the availability of D-Ala-D-Ala termini from the cell surface, which constitute the antibiotic target residues. {ECO:0000269|PubMed:8631706}. |
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| Cofactor: | |
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:30016658}; |
| Activity regulation: | |
Carboxypeptidase activity is insensitive to beta- lactams since it is not affected by penicillin G or ampicillin and is inhibited only by very high concentrations of cefalotin and cefoxitin. {ECO:0000269|PubMed:8631706}. |
| Subunit: | |
Monomer. {ECO:0000269|PubMed:30016658}. |
| Subcellular location: | |
Cell membrane {ECO:0000305|PubMed:8631706}; Single-pass membrane protein {ECO:0000255}. |
| Induction: | |
By vancomycin, mediated by VanS/VanR. Part of the VanB-type operon associated to vancomycin resistance in E.faecalis V583. {ECO:0000269|PubMed:8631706}. |
| Similarity: | |
Belongs to the peptidase M15B family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.