PROSITE documentation PDOC00357
Prokaryotic zinc-dependent phospholipase C domain signature and profile


Bacillus cereus expresses a phosphatidylcholine hydrolyzing phospholipase C (EC (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.


Technical section

PROSITE methods (with tools and information) covered by this documentation:

PROKAR_ZN_DEPEND_PLPC_2, PS51346; Prokaryotic zinc-dependent phospholipase C domain profile  (MATRIX)

PROKAR_ZN_DEPEND_PLPC_1, PS00384; Prokaryotic zinc-dependent phospholipase C signature  (PATTERN)


1AuthorsHough E. Hansen L.K. Birknes B. Jynge K. Hansen S. Hordvik A. Little C. Dodson E. Derewenda Z.
TitleHigh-resolution (1.5 A) crystal structure of phospholipase C from Bacillus cereus.
SourceNature 338:357-360(1989).
PubMed ID2493587

2AuthorsTitball R.W. Rubidge T.
TitleThe role of histidine residues in the alpha toxin of Clostridium perfringens.
SourceFEMS Microbiol. Lett. 56:261-265(1990).
PubMed ID2111259

3AuthorsVazquez-Boland J.A. Dominguez L. Rodriguez-Ferri E.F. Fernandez-Garayzabal J.F. Suarez G.
TitlePreliminary evidence that different domains are involved in cytolytic activity and receptor (cholesterol) binding in listeriolysin O, the Listeria monocytogenes thiol-activated toxin.
SourceFEMS Microbiol. Lett. 53:95-99(1989).
PubMed ID2515103

4AuthorsNaylor C.E. Eaton J.T. Howells A. Justin N. Moss D.S. Titball R.W. Basak A.K.
TitleStructure of the key toxin in gas gangrene.
SourceNat. Struct. Biol. 5:738-746(1998).
PubMed ID9699639

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