CATH Classification
Level | CATH Code | Description |
---|---|---|
1 | Mainly Alpha | |
1.10 | Orthogonal Bundle | |
1.10.1780 | Double Clp-N motif | |
1.10.1780.10 | Clp, N-terminal domain |
Domain Context
CATH Clusters
Superfamily | Clp, N-terminal domain |
Functional Family | ATP-dependent Clp protease ATP-binding subunit |
Enzyme Information
3.4.21.92 |
Endopeptidase Clp.
based on mapping to UniProt P0ABH9
Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. Alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec; and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).
-!- Belongs to peptidase family S14.
|
UniProtKB Entries (1)
P0ABH9 |
CLPA_ECOLI
Escherichia coli K-12
ATP-dependent Clp protease ATP-binding subunit ClpA
|
PDB Structure
PDB | 1K6K |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | Escherichia |
Primary Citation |
Crystal structure of ClpA, an HSP100 chaperone and regulator of ClpAP protease
J.Biol.Chem.
|