Zinc-dependent phospholipase C (IPR001531)
Short name: Zn_PLipaseC
Overlapping homologous superfamilies
- Phospholipase C/P1 nuclease domain superfamily (IPR008947)
Bacillus cereus contains a monomeric phospholipase C EC:188.8.131.52 (PLC) of 245 amino-acid residues that binds three zinc ions [PMID: 2493587]. Although PLC prefers to act on phosphatidylcholine, it also shows weak catalytic activity with sphingomyelin and phosphatidylinositol [PMID: 2841128]. Sequence studies have shown the PLC protein to be similar to the following:
- Alpha toxin from Clostridium perfringens and Clostridium bifermentans, which are zinc-dependent phospholipases C involved in haemolysis and cell rupture [PMID: 2536355].
- Lecithinase C from Listeria monocytogenes, which aids cell-to-cell spread by breaking down the 2-membrane vacuoles that surround the bacterium during transfer [PMID: 1309513].
Each of these proteins is a zinc-dependent enzyme, binding 3 zinc ions per molecule [PMID: 2111259]. The enzymes catalyse the conversion of phosphatidylcholine and water to 1,2-diacylglycerol and choline phosphate [PMID: 2841128, PMID: 2536355, PMID: 2111259]. In B. cereus, there are nine residues known to be involved in binding the zinc ions: 5 His, 2 Asp, 1 Glu and 1 Trp. These residues are all conserved in the Clostridium alpha-toxin [PMID: 9699639].
- PS00384 (PROKAR_ZN_DEPEND_PLPC_1)
- PS51346 (PROKAR_ZN_DEPEND_PLPC_2)
- SM00770 (Zn_dep_PLPC)
- PR00479 (PRPHPHLPASEC)
- cd11009 (Zn_dep_PLPC)
- PD003946 (PLipaseC_Zn-bd_prok)