Member database | PROSITE patterns |
PROSITE patterns type | conserved site |
Short name | CLP_PROTEASE_SER |
Description
The endopeptidase Clp (EC 3.4.21.92) 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.
References
1.Clp P represents a unique family of serine proteases. Maurizi MR, Clark WP, Kim SH, Gottesman S. J. Biol. Chem. 265, 12546-52, (1990). View articlePMID: 2197276
2.Regulation by proteolysis: energy-dependent proteases and their targets. Gottesman S, Maurizi MR. Microbiol. Rev. 56, 592-621, (1992). View articlePMID: 1480111