Zinc-dependent phospholipase C (IPR001531)

Short name: Zn_PLipaseC

Overlapping homologous superfamilies

Domain relationships



Bacillus cereus contains a monomeric phospholipase C EC: (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].

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0004629 phospholipase C activity
GO:0008270 zinc ion binding

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE patterns
PROSITE profiles