Secreted, cytolytic toxin that forms pores in host membranes after proteolytic removal of a C-terminal propeptide, leading to destruction of the membrane permeability barrier and host cell death. The pores are formed by transmembrane beta-strands and are approximately 3 nm in diameter. Homodimer in solution; homoheptamer in the host membrane. After binding to GPI-anchored proteins in target membranes and proteolytic removal of the C-terminal propeptide, the protein assembles into a heptameric pre-pore complex. A further conformation change leads to insertion into the host membrane. Secreted as a soluble precursor. The C-terminal propeptide is required for normal protein folding and secretion; it maintains the aerolysin precursor in its soluble form and prevents premature heptamerization and pore formation. Proteolytic cleavage and subsequent release of the propeptide trigger a major conformation change, leading to the formation of a heptameric pre-pore that then inserts into the host membrane. Belongs to the aerolysin family.