{PDOC60030} {PS60030; BACTERIOCIN_IIA} {BEGIN} ****************************************** * Bacteriocin class IIa family signature * ****************************************** 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 [1-3]. 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 beta-sheet supported by the conserved disulfide bridge (see ). 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 (see ) 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: - Pediococcus acidilactici pediocin PA-1. - Leuconostoc mesenteroides mesentericin Y105. - Carnobacterium piscicola carnobacteriocin B2. - Lactobacillus sake sakacin P. - Enterococcus faecium enterocin A. - Enterococcus faecium enterocin P. - Leuconostoc gelidum leucocin A. - Lactobacillus curvatus curvacin A. - Listeria innocua listeriocin 743A. The pattern we developed for the class IIa bacteriocin family covers the 'pediocin box' motif. -Conserved pattern: Y-G-N-G-[VL]-x-C-x(4)-C -Sequences known to belong to this class detected by the pattern: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Expert(s) to contact by email: Ramakumar S.; ramak@physics.iisc.ernet.in -Last update: March 2006 / First entry. [ 1] Ennahar S., Sonomoto K., Ishizaki A. "Class IIa bacteriocins from lactic acid bacteria: antibacterial activity and food preservation." J. Biosci. Bioeng. 87:705-716(1999). PubMed=16232543 [ 2] Johnsen L., Fimland G., Nissen-Meyer J. "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." J. Biol. Chem. 280:9243-9250(2005). PubMed=15611086; DOI=10.1074/jbc.M412712200 [ 3] Fimland G., Johnsen L., Dalhus B., Nissen-Meyer J. "Pediocin-like antimicrobial peptides (class IIa bacteriocins) and their immunity proteins: biosynthesis, structure, and mode of action." J. Pept. Sci. 11:688-696(2005). PubMed=16059970; DOI=10.1002/psc.699 -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}