| Primary Identifier | IPR027279 | Type | Homologous_superfamily |
| Short Name | D_amino_pept/lipop_sf |
| description | Beta-Lactam antibiotics interfere with the biosynthesis of peptidoglycans in the bacterial cell wall by inactivating the penicillin-binding proteins DD-transpeptidases. Bacterial resistance to beta-lactam occurs through the synthesis of beta-lactmases that hydrolyse beta-lactam rings. D-aminopeptidase (DAP; peptidase family S12) is inhibited by beta-lactam antibiotics, and shares a low sequence identity with class C beta-lactamases and R61 DD-carboxypeptidase. DAP consists of three domains: the N-terminal domain A contains catalytic residues and displays a beta-lactamase-like fold (), domains B (middle) and C (C-terminal) domains are structurally similar, displaying an eight-stranded beta barrel []. Domain C is responsible for substrate and inhibitor specificity.This superfamily represents a structurally similar domain to domains B and C of D-aminopeptidase. Proteins in this entry include D-aminopeptidases and some uncharacterised hypothetical lipoproteins from Streptococcus. |
