Metalloproteases including zinc D-Ala-D-Ala carboxypeptidase, L-Ala-D-Glu peptidase, L,D-carboxypeptidase, bacteriophage endolysins, and related proteins
This family summarizes zinc-binding metallopeptidases which are mostly carboxypeptidases and dipeptidases, and includes zinc-dependent D-Ala-D-Ala carboxypeptidases, VanX, L-Ala-D-Glu peptidase, L,D-carboxypeptidase and bacteriophage endolysins, amongst other family members. These peptidases belong to MEROPS family M15 which are involved in bacterial cell wall biosynthesis and metabolism.
Feature 1: active site [active site], 5 residue positions
Conserved feature residue pattern:R H D [ED] H
Evidence:
Comment:based on structures of Enterococcus faecalis D,D-dipeptidase VanXYg and Enterococcus faecium VanX and on mutagenesis studies
Structure:4MUQ: Enterococcus faecalis vancomycin-resistance D,D-dipeptidase VanXYg binds D-ala-D-ala phosphinate analog and a zinc ion, contacts at 4A - View structure with Cn3D
Structure:1R44: Enterococcus faecium vanX binds zinc ion - View structure with Cn3D
Jiyao W et al.(2023). "The conserved domain database in 2023.",