PROSITE documentation PDOC00357Prokaryotic zinc-dependent phospholipase C domain signature and profile
Bacillus cereus expresses a phosphatidylcholine hydrolyzing phospholipase C (EC 3.1.4.3) (PLC) which is a monomeric protein of 245 amino-acid residues that binds three zinc ions [1]. This PLC is highly similar to the following proteins:
- α-toxin from Clostridium perfringens and bifermentans which are also zinc-dependent phospholipases C [2].
- Lecithinase C from Listeria monocytogenes [3].
In Bacillus 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 α-toxin [4].
As a signature pattern for this family of enzymes, we selected a conserved region of 11 residues that contains three of the zinc ligands: a histidine involved in binding the first zinc ion, an aspartic acid which binds both the first and the third zinc ion, and a histidine which binds the second zinc ion. We also developed a profile that covers the entire prokaryotic zinc-dependent phospholipase C domain.
Last update:December 2007 / Text revised; profile added.
-------------------------------------------------------------------------------
PROSITE methods (with tools and information) covered by this documentation:
| 1 | Authors | Hough E. Hansen L.K. Birknes B. Jynge K. Hansen S. Hordvik A. Little C. Dodson E. Derewenda Z. |
| Title | High-resolution (1.5 A) crystal structure of phospholipase C from Bacillus cereus. | |
| Source | Nature 338:357-360(1989). | |
| PubMed ID | 2493587 | |
| DOI | 10.1038/338357a0 |
| 2 | Authors | Titball R.W. Rubidge T. |
| Title | The role of histidine residues in the alpha toxin of Clostridium perfringens. | |
| Source | FEMS Microbiol. Lett. 56:261-265(1990). | |
| PubMed ID | 2111259 |
| 3 | Authors | Vazquez-Boland J.A. Dominguez L. Rodriguez-Ferri E.F. Fernandez-Garayzabal J.F. Suarez G. |
| Title | Preliminary evidence that different domains are involved in cytolytic activity and receptor (cholesterol) binding in listeriolysin O, the Listeria monocytogenes thiol-activated toxin. | |
| Source | FEMS Microbiol. Lett. 53:95-99(1989). | |
| PubMed ID | 2515103 |
| 4 | Authors | Naylor C.E. Eaton J.T. Howells A. Justin N. Moss D.S. Titball R.W. Basak A.K. |
| Title | Structure of the key toxin in gas gangrene. | |
| Source | Nat. Struct. Biol. 5:738-746(1998). | |
| PubMed ID | 9699639 | |
| DOI | 10.1038/1447 |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.
View entry in original PROSITE document format
View entry in raw text format (no links)