{PDOC00357} {PS00384; PROKAR_ZN_DEPEND_PLPC_1} {PS51346; PROKAR_ZN_DEPEND_PLPC_2} {BEGIN} *************************************************************************** * Prokaryotic 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: - Alpha-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 alpha-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. -Consensus pattern: H-Y-x-[GT]-D-[LIVMAF]-[DNSH]-x-P-x-H-[PA]-x-N [The 2 H's and the D bind zinc] -Sequences known to belong to this class detected by the pattern: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Sequences known to belong to this class detected by the profile: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: December 2007 / Text revised; profile added. [ 1] Hough E., Hansen L.K., Birknes B., Jynge K., Hansen S., Hordvik A., Little C., Dodson E., Derewenda Z. "High-resolution (1.5 A) crystal structure of phospholipase C from Bacillus cereus." Nature 338:357-360(1989). PubMed=2493587; DOI=10.1038/338357a0 [ 2] Titball R.W., Rubidge T. "The role of histidine residues in the alpha toxin of Clostridium perfringens." FEMS Microbiol. Lett. 56:261-265(1990). PubMed=2111259 [ 3] Vazquez-Boland J.A., Dominguez L., Rodriguez-Ferri E.F., Fernandez-Garayzabal J.F., Suarez G. "Preliminary evidence that different domains are involved in cytolytic activity and receptor (cholesterol) binding in listeriolysin O, the Listeria monocytogenes thiol-activated toxin." FEMS Microbiol. Lett. 53:95-99(1989). PubMed=2515103 [ 4] Naylor C.E., Eaton J.T., Howells A., Justin N., Moss D.S., Titball R.W., Basak A.K. "Structure of the key toxin in gas gangrene." Nat. Struct. Biol. 5:738-746(1998). PubMed=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 https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}