A cholesterol-dependent toxin that causes cytolysis by forming pores in cholesterol containing host membranes. After binding to target membranes, the protein undergoes a major conformation change, leading to its insertion in the host membrane and formation of an oligomeric pore complex. Cholesterol is required for binding to host membranes, membrane insertion and pore formation; cholesterol binding is mediated by a Thr-Leu pair in the C-terminus. Can be reversibly inactivated by oxidation. Homooligomeric pore complex of 35 to 50 subunits; when inserted in the host membrane. Probably secreted as soluble protein by the accessory Sec system (By similarity). It then inserts into the host cell membrane and forms pores formed by transmembrane beta-strands (By similarity). Mature protein (about residues 103 to 571) has 3 discontinuous domains; D1 (residues 103-124, 161-249, 300-345 and 421-444), D2 (residues 125-160 and 445-461), D3 (residues 250-299 and 346-420) followed by C-terminal D4 (residues 462-571). Belongs to the cholesterol-dependent cytolysin family. Truncated N-terminus.