A0A1S6WS70 · A0A1S6WS70_9HYPH
- ProteinATP-dependent protease ATPase subunit HslU
- GenehslU
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids436 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. 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.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 19 | ATP (UniProtKB | ChEBI) | |||
Binding site | 249 | ATP (UniProtKB | ChEBI) | |||
Binding site | 314 | ATP (UniProtKB | ChEBI) | |||
Binding site | 386 | ATP (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | HslUV protease complex | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | peptidase activity | |
Molecular Function | proteasome-activating activity | |
Biological Process | protein unfolding | |
Biological Process | proteolysis involved in protein catabolic process |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended nameATP-dependent protease ATPase subunit HslU
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Bartonellaceae > Bartonella
Accessions
- Primary accessionA0A1S6WS70
Proteomes
Subcellular Location
Interaction
Subunit
A double ring-shaped homohexamer of HslV is capped on each side by a ring-shaped HslU homohexamer. The assembly of the HslU/HslV complex is dependent on binding of ATP.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 50-325 | AAA+ ATPase | |||
Domain | 328-422 | Clp ATPase C-terminal | |||
Sequence similarities
Belongs to the ClpX chaperone family. HslU subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length436
- Mass (Da)48,303
- Last updated2017-05-10 v1
- ChecksumA4A915935B3E79F5
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP019781 EMBL· GenBank· DDBJ | AQX19161.1 EMBL· GenBank· DDBJ | Genomic DNA |