Serine protease that hydrolyzes large proteins such as casein and gelatin. Cleaves preferentially at the carboxyl terminus of Phe, Tyr or Leu (PubMed:10879563). Is also able to catalyze peptide synthesis under different salt concentrations in the presence of dimethyl sulfoxide (DMSO) (PubMed:21039670). Dependent on high salt concentrations for activity and stability. Strongly inhibited by the serine protease inhibitors diisopropyl fluorophosphate (DFP), phenylmethyl sulfonylfluoride (PMSF) and chymostatin. Also inhibited by denaturing agents such as SDS, urea, and HCl guanidinium. Activated by thiol-containing reducing agents such as dithiotreitol (DTT) and 2-mercaptoethanol. Optimum pH is 8-10. Optimum temperature is 60 degrees Celsius. Monomer. Expressed and secreted during the transition to the stationary growth phase. Is probably up-regulated in response to factors (metabolite and/or regulatory molecule) occurring in high-density cultures. Exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven. After transport across the membrane, the propeptide is probably processed autocatalytically, yielding the mature fully active protease. Belongs to the peptidase S8 family.