Intracellular serine protease 1 of Bacillus subtilis is formed in vivo as an unprocessed, active protease in stationary cells.
Western immunoblots and assays of Bacillus subtilis extracts showed that intracellular serine protease 1 is produced in a form larger than previously reported, appears not to have undergone N-terminal processing, and is active in the presence or absence of calcium. No evidence for an inactive precursor form of the protease was found.
Sheehan
S M
SM
Department of Biochemistry, University of Illinois, Urbana 61801.
Switzer
R L
RL
D001412:Bacillus subtilis / Q000201:enzymology*; D002118:Calcium / Q000494:pharmacology; D004792:Enzyme Precursors / Q000032:analysis; D015151:Immunoblotting; D012697:Serine Endopeptidases / Q000032:analysis / Q000096:biosynthesis* / Q000302:isolation & purification
D004792:Enzyme Precursors; D012697:Serine Endopeptidases; D002118:Calcium