PROSITE documentation PDOC00358
Endopeptidase Clp active sites


The endopeptidase Clp (EC from Escherichia coli cleaves peptides in various proteins in a process that requires ATP hydrolysis [1,2]. Clp is a dimeric protein which consists of a proteolytic subunit (gene clpP) and either of two related ATP-binding regulatory subunits (genes clpA and clpX). ClpP is a serine protease which has a chymotrypsin-like activity. Its catalytic activity seems to be provided by a charge relay system similar to that of the trypsin family of serine proteases, but which evolved by independent convergent evolution.

Proteases highly similar to ClpP have been found to be encoded in the genome of the chloroplast of plants and seem to be also present in other eukaryotes.

The sequences around two of the residues involved in the catalytic triad (a serine and a histidine) are highly conserved and can be used as signature patterns specific to that category of proteases.


These proteins belong to family S14 in the classification of peptidases [3,E1].

Last update:

December 2001 / Patterns and text revised.


Technical section

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

CLP_PROTEASE_HIS, PS00382; Endopeptidase Clp histidine active site  (PATTERN)

CLP_PROTEASE_SER, PS00381; Endopeptidase Clp serine active site  (PATTERN)


1AuthorsMaurizi M.R. Clark W.P. Kim S.-H. Gottesman S.
TitleClp P represents a unique family of serine proteases.
SourceJ. Biol. Chem. 265:12546-12552(1990).
PubMed ID2197276

2AuthorsGottesman S. Maurizi M.R.
TitleRegulation by proteolysis: energy-dependent proteases and their targets.
SourceMicrobiol. Rev. 56:592-621(1992).
PubMed ID1480111

3AuthorsRawlings N.D. Barrett A.J.
TitleFamilies of serine peptidases.
SourceMethods Enzymol. 244:19-61(1994).
PubMed ID7845208


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