Serine protease capable of cleaving pepsin A and human coagulation factor V, which may contribute to the mucosal hemorrhage observed in hemorrhagic colitis. Inhibition of cytotoxic activity by phenylmethylsulfonyl fluoride. The cleaved C-terminal fragment (autotransporter domain) is localized in the outer membrane. Expression is optimal at 37 degrees Celsius, and inhibited at 20 degrees Celsius. It is dependent on both temperature and pH. The signal peptide, cleaved at the inner membrane, guides the autotransporter protein to the periplasmic space. Then, insertion of the C-terminal translocator domain in the outer membrane forms a hydrophilic pore for the translocation of the passenger domain to the bacterial cell surface, with subsequent cleavage (PubMed:15615856). Cleaved to release the mature protein from the outer membrane. Mutagenesis experiments show the presence of a linker region, which is required for the translocation of the protease domain across the outer membrane. This linker region is located immediately upstream of the C-terminal helper domain. The signal peptide may also act as a transient membrane anchor that prevents the protease domain from misfolding in the periplasm. Strain 3010/96 exhibits a partial deletion of the gene.