Autotransporter serine protease probably involved in virulence. Inhibited by phenylmethylsulfonyl fluoride. The cleaved C-terminal fragment (autotransporter domain) is localized in the outer membrane. 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 (Probable). Cleaved to release the mature protein from the outer membrane. Leads to accelerated virulence in the rabbit ileal loop model of infection. Nevertheless, the relationship between the enzymatic and potential virulence functions is uncertain.