PROSITE documentation PDOC60030

Bacteriocin class IIa family signature

Description:

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:

  • 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.

Expert(s) to contact by email:

Ramakumar S.

Last update:

March 2006 / First entry.

Technical section:

PROSITE method (with tools and information) covered by this documentation:

BACTERIOCIN_IIA, PS60030Bacteriocin class IIa family signature  (PATTERN)
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.
• Retrieve an alignment of Swiss-Prot true positive hits:
  Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format
Retrieve the sequence logo from the alignment
Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS60030
Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS60030
Scan Swiss-Prot/TrEMBL entries against PS60030
view ligand binding statistics

References:

1 AuthorsEnnahar S., Sonomoto K., Ishizaki A.
TitleClass IIa bacteriocins from lactic acid bacteria: antibacterial activity and food preservation.
SourceJ. Biosci. Bioeng. 87:705-716(1999).
PubMed ID16232543
2 AuthorsJohnsen L., Fimland G., Nissen-Meyer J.
TitleThe 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.
SourceJ. Biol. Chem. 280:9243-9250(2005).
PubMed ID15611086
DOI10.1074/jbc.M412712200
3 AuthorsFimland G., Johnsen L., Dalhus B., Nissen-Meyer J.
TitlePediocin-like antimicrobial peptides (class IIa bacteriocins) and their immunity proteins: biosynthesis, structure, and mode of action.
SourceJ. Pept. Sci. 11:688-696(2005).
PubMed ID16059970
DOI10.1002/psc.699

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