CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.50 | Rossmann fold |
|
3.40.50.300 | P-loop containing nucleotide triphosphate hydrolases |
Domain Context
CATH Clusters
| Superfamily | P-loop containing nucleotide triphosphate hydrolases |
| Functional Family | ATP-dependent protease (Clp chaperone) |
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 | 1KSF |
| 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.
|