Serine protease with enterotoxic and cytotoxic activities. Cleaves fodrin, but does not cause its redistribution within epithelial cells. The exact role of EspC in EPEC pathogenesis is still unknown. Inhibition of cytotoxic activity by phenylmethylsulfonyl fluoride. The cleaved C-terminal fragment (autotransporter domain) is localized in the outer membrane. Expression is repressed by glucose. 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.