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| PROSITE documentation PDOC00358 |
Endopeptidase Clp active sites
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.
Note:
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) |
| Consensus pattern: |
R-x(3)-[EAP]-x(3)-[LIVMFYT]-[LM]-[LIVM]-H-Q-P
H is the active site residue |
| Sequences known to belong to this class detected by the pattern: |
ALL, except two sequences |
| Other sequence(s) detected in Swiss-Prot: |
1. |
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| Matching PDB structures:
1R8V 1R8Z 1R90 1R91 ... [ALL] |
| CLP_PROTEASE_SER, PS00381; Endopeptidase Clp serine active site (PATTERN) |
| Consensus pattern: |
T-x(2)-[LIVMF]-G-x-A-[SAC]-S-[MSA]-[PAG]-[STA]
S is the active site residue |
| Sequences known to belong to this class detected by the pattern: |
ALL, except three sequences |
| Other sequence(s) detected in Swiss-Prot: |
2. |
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| Matching PDB structures:
1R8V 1R90 1R92 1TG6 ... [ALL] |
References:
| 1 |
Authors | Maurizi M.R., Clark W.P., Kim S.-H., Gottesman S. |
| Title | Clp P represents a unique family of serine proteases. |
| Source | J. Biol. Chem. 265:12546-12552(1990). |
| PubMed ID | 2197276 |
| 2 |
Authors | Gottesman S., Maurizi M.R. |
| Title | Regulation by proteolysis: energy-dependent proteases and their targets. |
| Source | Microbiol. Rev. 56:592-621(1992). |
| PubMed ID | 1480111 |
| 3 |
Authors | Rawlings N.D., Barrett A.J. |
| Title | Families of serine peptidases. |
| Source | Methods Enzymol. 244:19-61(1994). |
| PubMed ID | 7845208 |
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