Molecular cloning and sequence analysis of a gene encoding an extracellular serine protease from Streptomyces lividans 66

Biosci Biotechnol Biochem. 1995 Jul;59(7):1386-8. doi: 10.1271/bbb.59.1386.

Abstract

A gene encoding a homolog of the chymotrypsin-like serine protease (SAM-P20), which was isolated as the target enzyme of a protease inhibitor (SSI), was cloned from Streptomyces lividans 66. This gene contained an open reading frame of 1065 nucleotides encoding 354 amino acid residues with a putative prepro portion of 157 amino acid residues. The deduced amino acid sequence of the cloned gene had significant homology to those of members of Streptomyces extracellular chymotrypsin-like protease family. By Southern blot analysis, it was suggested that protease genes of this type are found at a high frequency in Streptomyces. In this sense, we propose to categorize this protease as a member of the 'SAL' series (SAM-P20-like proteases).

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Blotting, Southern
  • Cloning, Molecular
  • Molecular Sequence Data
  • Open Reading Frames
  • Serine Endopeptidases / biosynthesis*
  • Serine Endopeptidases / genetics*
  • Streptomyces / enzymology*
  • Streptomyces / genetics*

Substances

  • Serine Endopeptidases

Associated data

  • GENBANK/S79442