| Primary Identifier | IPR033135 | Type | Active_site |
| Short Name | ClpP_His_AS |
| description | The endopeptidase Clp () from Escherichia coli cleaves peptides invarious proteins in a process that requires ATP hydrolysis [, ]. Clp is adimeric protein which consists of a proteolytic subunit (gene clpP) and eitherof two related ATP-binding regulatory subunits (genes clpA and clpX). ClpP isa serine protease which has a chymotrypsin-like activity. Its catalyticactivity seems to be provided by a charge relay system similar to that of thetrypsin family of serine proteases, but which evolved by independentconvergent evolution.Proteases highly similar to ClpP have been found to be encoded in the genomeof the chloroplast of plants and seem to be also present in other eukaryotes.This entry represents a conserved region containing a histidine that is involved in the catalytic triad. |
