A cholesterol-dependent toxin that causes cytolysis by forming pores in cholesterol containing host membranes (Probable). 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. Secreted as soluble protein by the accessory Sec system (PubMed:28456649). It then inserts into the host cell membrane and forms pores formed by transmembrane beta-strands (By similarity). Has a slightly altered apparent molecular weight in a secA2 deletion mutant, but no post-translational modifications have been found. No change in biofilm formation, about 35% decreased adherence to human lung pneumocytes. Complete loss of host cell hemolytic activity. Belongs to the cholesterol-dependent cytolysin family.