Q6N5L4 · CLPX_RHOPA
- ProteinATP-dependent Clp protease ATP-binding subunit ClpX
- GeneclpX
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids424 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 15 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 18 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 37 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 40 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 119-126 | ATP (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | HslUV protease complex | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | ATP-dependent protein folding chaperone | |
Molecular Function | protein dimerization activity | |
Molecular Function | unfolded protein binding | |
Molecular Function | zinc ion binding | |
Biological Process | cell division | |
Biological Process | proteolysis involved in protein catabolic process |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended nameATP-dependent Clp protease ATP-binding subunit ClpX
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Nitrobacteraceae > Rhodopseudomonas
Accessions
- Primary accessionQ6N5L4
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000160411 | 1-424 | ATP-dependent Clp protease ATP-binding subunit ClpX | ||
Interaction
Subunit
Component of the ClpX-ClpP complex. Forms a hexameric ring that, in the presence of ATP, binds to fourteen ClpP subunits assembled into a disk-like structure with a central cavity, resembling the structure of eukaryotic proteasomes.
Protein-protein interaction databases
Structure
Family & Domains
Sequence
- Sequence statusComplete
- Length424
- Mass (Da)46,680
- Last updated2004-07-05 v1
- MD5 Checksum3C4FE8C899CF364ACD9B175621A439D4
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BX572602 EMBL· GenBank· DDBJ | CAE28401.1 EMBL· GenBank· DDBJ | Genomic DNA |