Bacterial hemolysins are exotoxins that attack blood cell membranes and cause cell rupture. Binds to eukaryotic membranes where it hydrolyzes phosphatidylcholine, sphingomyelin and phosphatidylethanolamine. The diacylglycerol produced can activate both the arachidonic acid pathway, leading to modulation of the inflammatory response cascade and thrombosis, and protein kinase C, leading to activation of eukaryotic phospholipases and further membrane damage (By similarity). a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-sn-glycerol + H(+) + phosphocholine Binds 3 Ca(2+) ions. Binds 3 Zn(2+) ions. The protein is composed of 2 domains; the N-terminal domain contains the phospholipase C active site (PLC), in a cleft which is also occupied by the 3 zinc ions. The C-terminal domain is a putative phospholipid-recognition domain, which shows structural homology with phospholipid-binding C2-like domains from a range of eukaryotic proteins. The ability to bind membrane phospholipids in a Ca(2+) dependent manner and toxicity is conferred by this C-terminal domain, which also contributes to the sphingomyelinase activity (By similarity). Belongs to the bacterial zinc-metallophospholipase C family.