Zn_dep_PLPC

Zinc dependent phospholipase C (alpha toxin)
Zn_dep_PLPC
SMART accession number:SM00770
Description: This domain conveys a zinc dependent phospholipase C activity (EC 3.1.4.3). It is found in a monomeric phospholipase C of Bacillus cereus as well as in the alpha toxin of Clostridium perfringens and Clostridium bifermentans, which is involved in haemolysis and cell rupture. It is also found in a lecithinase of Listeria monocytogenes, which is involved in breaking the 2-membrane vacuoles that surround the bacterium. Structure information: PDB 1ca1.
Interpro abstract (IPR001531):

Bacillus cereus contains a monomeric phospholipase C EC 3.1.4.3 (PLC) of 245 amino-acid residues that binds three zinc ions [ (PUBMED:2493587) ]. Although PLC prefers to act on phosphatidylcholine, it also shows weak catalytic activity with sphingomyelin and phosphatidylinositol [ (PUBMED: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 [ (PUBMED: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 [ (PUBMED:1309513) ].

Each of these proteins is a zinc-dependent enzyme, binding 3 zinc ions per molecule [ (PUBMED:2111259) ]. The enzymes catalyse the conversion of phosphatidylcholine and water to 1,2-diacylglycerol and choline phosphate [ (PUBMED:2841128) (PUBMED:2536355) (PUBMED: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 [ (PUBMED:9699639) ].

GO function:phospholipase C activity (GO:0004629), zinc ion binding (GO:0008270)
Family alignment:
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There are 729 Zn_dep_PLPC domains in 729 proteins in SMART's nrdb database.

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