InterPro domain: IPR012338

This superfamily represents a beta-lactamase structural motif, which contains a cluster of alpha-helices and an alpha/beta sandwich. In addition to beta-lactamases, this domain is also found in D-ala carboxypeptidase/transpeptidase, esterase (EstB) [ 1 ], the penicillin receptor BlaR (C-terminal domain), D-aminopeptidase (N-terminal domain) [ 2 ], penicillin-biding proteins (e.g. PBP2x, PBP5), and in glutaminase (GlnA). Beta-lactamases are the most common bacterial resistance mechanism against beta-lactam antibiotics [ 3 ]. Beta-lactamases appear to have evolved from DD-transpeptidases, which are penicillin-binding proteins involved in cell wall biosynthesis, and as such are one of the main targets of beta-lactam antibiotics.

1. EstB from Burkholderia gladioli: a novel esterase with a beta-lactamase fold reveals steric factors to discriminate between esterolytic and beta-lactam cleaving activity. Protein Sci. 11, 467-78
2. Crystal structure of a D-aminopeptidase from Ochrobactrum anthropi, a new member of the 'penicillin-recognizing enzyme' family. Structure 8, 971-80
3. Understanding the acylation mechanisms of active-site serine penicillin-recognizing proteins: a molecular dynamics simulation study. Proteins 53, 88-100