PS00381

Endopeptidase Clp serine active site

PROSITE patterns entry
Member databasePROSITE patterns
PROSITE patterns typeconserved site
Short nameCLP_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

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