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. 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. Monomer. By vancomycin, mediated by VanS/VanR. Part of the VanB-type operon associated to vancomycin resistance in E.faecalis V583. Belongs to the peptidase M15B family.