Homologous Superfamily

Penicillin-binding protein, C-terminal domain superfamily (IPR015956)

Short name: Peniciliin-bd_prot_C_sf

Overlapping entries


This superfamily represents a structural motif found at the C-terminal of penicillin-binding proteins 4 (PBP4) and 5 (PBP5), as well as at the C-terminal of D-Ala-D-Ala carboxypeptidase A, a member of the MEROPS S11 peptidase family (PBP4 and PBP5 also belong to this peptidase family). These domains share a similar structure, consisting of a beta-sandwich of six strands in two sheets [PMID: 14555648, PMID: 15596446].

Penicillin-binding proteins are beta-lactam antibiotic-sensitive bacterial enzymes required for the growth and maintenance of the peptidoglycan layer of the bacterial cell wall that protects the cell from osmotic stress. PBP4 functions as a transpeptidase, acting co-operatively with PBP2 in staphylococcal cell wall biosynthesis and susceptibility to antimicrobial agents [PMID: 16411754].

GO terms

Biological Process

GO:0006508 proteolysis

Molecular Function

GO:0004180 carboxypeptidase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.