|PROSITE documentation PDOC60030 [for PROSITE entry PS60030]|
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 [1,2,3].
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 disulfide bridge. It forms a three-stranded antiparallel β-sheet supported by the conserved disulfide bridge (see <PDB:1OG7>). This cationic N-terminal β-sheet domain mediates binding of the class IIa bacteriocin to the target cell membrane. The C-terminal region forms a hairpin-like domain (see <PDB:1OG7>) 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 [2,3].
Some proteins known to belong to the class IIa bacteriocin family are listed below:
The pattern we developed for the class IIa bacteriocin family covers the 'pediocin box' motif.Expert(s) to contact by email:
March 2006 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Ennahar S. Sonomoto K. Ishizaki A.|
|Title||Class IIa bacteriocins from lactic acid bacteria: antibacterial activity and food preservation.|
|Source||J. Biosci. Bioeng. 87:705-716(1999).|
|2||Authors||Johnsen L. Fimland G. Nissen-Meyer J.|
|Title||The C-terminal domain of pediocin-like antimicrobial peptides (class IIa bacteriocins) is involved in specific recognition of the C-terminal part of cognate immunity proteins and in determining the antimicrobial spectrum.|
|Source||J. Biol. Chem. 280:9243-9250(2005).|
|3||Authors||Fimland G. Johnsen L. Dalhus B. Nissen-Meyer J.|
|Title||Pediocin-like antimicrobial peptides (class IIa bacteriocins) and their immunity proteins: biosynthesis, structure, and mode of action.|
|Source||J. Pept. Sci. 11:688-696(2005).|