Domain

D-aminopeptidase/lipoprotein domain (IPR027279)

Short name: D_amino_pept/lipop

Domain relationships

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) 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 (IPR001466), domains B (middle) and C (C-terminal) domains are structurally similar, displaying an eight-stranded beta barrel [PMID: 10986464]. Domain C is responsible for substrate and inhibitor specificity.

This entry 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.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
GENE3D