Characterization and structure of genes for proteases A and B from Streptomyces griseus.
Protease A and protease B are extracellular proteins which are secreted by Streptomyces griseus. The genes encoding protease A (sprA) and protease B (sprB) were isolated from an S. griseus genomic library by using a synthetic oligonucleotide probe. Fragments containing sprA and sprB were characterized by hybridization and demonstration of proteolytic activity in Streptomyces lividans. Each DNA sequence contains a large open reading frame with the coding region of the mature protease situated at its carboxy terminus. The amino terminus of each reading frame appears to encode a 38-amino-acid signal peptide followed by a 76- or 78-amino-acid polypeptide, a propeptide, which is joined to the mature protease. Strong homology between the coding regions of the protease genes suggests that sprA and sprB originated by gene duplication.
D000595:Amino Acid Sequence; D001483:Base Sequence; D004269:DNA, Bacterial / Q000235:genetics; D010450:Endopeptidases / Q000032:analysis / Q000235:genetics*; D005798:Genes, Bacterial; D009693:Nucleic Acid Hybridization; D021382:Protein Sorting Signals / Q000235:genetics; D012697:Serine Endopeptidases; D013305:Streptomyces griseus / Q000201:enzymology / Q000235:genetics*
D004269:DNA, Bacterial; D021382:Protein Sorting Signals; D010450:Endopeptidases; D012697:Serine Endopeptidases