Molecular cloning and sequence analysis of a gene encoding an extracellular serine protease from Streptomyces lividans 66.
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).
Taguchi
S
S
Department of Biological Science and Technology, Science University of Tokyo, Chiba, Japan.
Endo
T
T
Naoi
Y
Y
Momose
H
H
D000595:Amino Acid Sequence; D001483:Base Sequence; D015139:Blotting, Southern; D003001:Cloning, Molecular; D008969:Molecular Sequence Data; D016366:Open Reading Frames; D012697:Serine Endopeptidases / Q000096:biosynthesis* / Q000235:genetics*; D013302:Streptomyces / Q000201:enzymology* / Q000235:genetics*
D012697:Serine Endopeptidases