Conserved Site

Bacteriocin, class IIa, conserved site (IPR023384)

Short name: Bacteriocin_IIa_CS


Many Gram-positive bacteria produce ribosomally synthesized antimicrobial peptides, often termed bacteriocins. One important and well studied class of bacteriocins is the class IIa or pediocin-like bacteriocins produced by lactic acid bacteria. All class IIa bacteriocins are produced by food-associated strains, isolated from a variety of food products of industrial and natural origins, including meat products, dairy products and vegetables. Class IIa bacteriocins are all cationic, display anti-Listeria activity, and kill target cells by permeabilizing the cell membrane [PMID: 16232543, PMID: 15611086, PMID: 16059970].

Class IIa bacteriocins contain between 37 and 48 residues. Based on their primary structures, the peptide chains of class IIa bacteriocins may be divided roughly into two regions: a hydrophilic, cationic and highly conserved N-terminal region, and a less conserved hydrophobic/amphiphilic C-terminal region. The N-terminal region contains the conserved Y-G-N-G-V/L 'pediocin box' motif and two conserved cysteine residues joined by a disulphide bridge. It forms a three-stranded antiparallel beta-sheet supported by the conserved disulphide bridge. This cationic N-terminal beta-sheet domain mediates binding of the class IIa bacteriocin to the target cell membrane. The C-terminal region forms a hairpin-like domain that penetrates into the hydrophobic part of the target cell membrane, thereby mediating leakage through the membrane. The two domains are joined by a hinge, which enables movement of the domains relative to each other [PMID: 15611086, PMID: 16059970].

This entry represents a conserved site that covers the 'pediocin box' motif of the class IIa bacteriocin family.

Contributing signatures

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