Bacterial hemolysin that causes cytolysis by forming heptameric pores in target host membranes. Monomer. Homoheptamer. After binding to target membranes the protein assembles into a heptameric pre-pore complex. Proteolytic cleavage triggers a conformation change that is required for membrane insertion and pore formation. In the hemolytic biotype El Tor the 80 kDa hemolysin precursor is secreted as monomer. After binding to target membranes the protein assembles into a heptameric prepore complex. Proteolytic cleavage triggers a conformation change that is required for membrane insertion and pore formation. By hemolysin B cytoplasmic protein. May bind to glycans on target cells via the C-terminal beta-prism domain. Proteolytical cleavage is required to convert the 80 kDa hemolysin precursor into the active 65 kDa hemolysin. Belongs to the HlyA hemolysin family.