CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.60 | 4-Layer Sandwich |
|
3.60.20 | Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 |
|
3.60.20.10 | Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 |
Domain Context
CATH Clusters
| Superfamily | Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 |
| Functional Family | ATP-dependent protease subunit HslV |
Enzyme Information
| 3.4.25.2 |
HslU--HslV peptidase.
based on mapping to UniProt B7LA29
ATP-dependent cleavage of peptide bonds with broad specificity.
-!- The HslU subunit of the HslU--HslV complex functions as an ATP dependent 'unfoldase'. -!- The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. -!- HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. -!- Belongs to peptidase family T1.
|
UniProtKB Entries (2)
| B7LA29 |
HSLV_ECO55
Escherichia coli 55989
ATP-dependent protease subunit HslV
|
| P0A6H6 |
HSLU_ECO57
Escherichia coli O157:H7
ATP-dependent protease ATPase subunit HslU
|
PDB Structure
| PDB | 5JI2 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
A Structurally Dynamic Region of the HslU Intermediate Domain Controls Protein Degradation and ATP Hydrolysis.
Structure
|
