Zn_dep_PLPCZinc dependent phospholipase C (alpha toxin)
|SMART accession number:||SM00770|
|Description:||This domain conveys a zinc dependent phospholipase C activity (EC 188.8.131.52). 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 184.108.40.206 (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:
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)|
Click on the following links for more information.
- Evolution (species in which this domain is found)
- Literature (relevant references for this domain)
- Metabolism (metabolic pathways involving proteins which contain this domain)
- Structure (3D structures containing this domain)
- Links (links to other resources describing this domain)