Characterization of a novel PepF-like oligopeptidase secreted by Bacillus amyloliquefaciens 23-7A

Appl Environ Microbiol. 2006 Jan;72(1):968-71. doi: 10.1128/AEM.72.1.968-971.2006.

Abstract

An oligopeptidase from Bacillus amyloliquefaciens 23-7A was characterized along with its biochemical activities and structural gene. The protein's amino acid sequence and enzymatic activities were similar to those of other bacterial PepFs, which belong to metallopeptidase family M3. While most bacterial PepFs are cytoplasmic endopeptidases, the identified PepFBa oligopeptidase is a secreted protein and may facilitate the process of sporulation.

MeSH terms

  • Amino Acid Sequence
  • Bacillus / enzymology*
  • Bacillus / genetics
  • Bacillus / physiology
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Bacterial Proteins / physiology
  • Metalloendopeptidases / chemistry*
  • Metalloendopeptidases / genetics
  • Metalloendopeptidases / metabolism*
  • Metalloendopeptidases / physiology
  • Molecular Sequence Data
  • Sequence Analysis, DNA
  • Substrate Specificity

Substances

  • Bacterial Proteins
  • Metalloendopeptidases
  • Oligoendopeptidase F

Associated data

  • GENBANK/AF525011