Molecular and genetic characterization of propionicin F, a bacteriocin from Propionibacterium freudenreichii

Appl Environ Microbiol. 2004 Dec;70(12):7303-10. doi: 10.1128/AEM.70.12.7303-7310.2004.


This work describes the purification and characterization of propionicin F, the first bacteriocin isolated from Propionibacterium freudenreichii. The bacteriocin has a bactericidal activity and is only active against strains of P. freudenreichii. Propionicin F appears to be formed through a processing pathway new to bacteriocins. The mass of the purified bacteriocin was determined by mass spectrometry, and the N-terminal amino acid sequence was determined by Edman degradation. Sequencing of pcfA, the bacteriocin structural gene, revealed that propionicin F corresponds to a 43-amino-acid peptide in the central part of a 255-amino-acid open reading frame, suggesting that mature propionicin F is excised from the probacteriocin by N- and C-terminal proteolytic modifications. DNA sequencing and Northern blot hybridizations revealed that pcfA is cotranscribed with genes encoding a putative proline peptidase and a protein from the radical S-adenosylmethionine family. A gene encoding an ABC transporter was also identified in close proximity to the bacteriocin structural gene. The potential role of these genes in propionicin F maturation and secretion is discussed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Anti-Bacterial Agents / pharmacology
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics*
  • Bacterial Proteins / metabolism*
  • Bacteriocins / chemistry*
  • Bacteriocins / metabolism*
  • Bacteriocins / pharmacology
  • Base Sequence
  • Microbial Sensitivity Tests
  • Molecular Sequence Data
  • Propionibacterium / drug effects
  • Propionibacterium / genetics
  • Propionibacterium / metabolism*
  • Sequence Analysis, DNA


  • Anti-Bacterial Agents
  • Bacterial Proteins
  • Bacteriocins

Associated data

  • GENBANK/AY587566