Q2RNA2 · Q2RNA2_RHORT
- ProteinATP-dependent protease subunit HslV
- GenehslV
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids187 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
Catalytic activity
Activity regulation
Allosterically activated by HslU binding.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Active site | 18 | ||||
Binding site | 172 | Na+ (UniProtKB | ChEBI) | |||
Binding site | 175 | Na+ (UniProtKB | ChEBI) | |||
Binding site | 178 | Na+ (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | HslUV protease complex | |
Cellular Component | proteasome core complex | |
Molecular Function | metal ion binding | |
Molecular Function | threonine-type endopeptidase activity | |
Biological Process | proteolysis involved in protein catabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameATP-dependent protease subunit HslV
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Rhodospirillales > Rhodospirillaceae > Rhodospirillum
Accessions
- Primary accessionQ2RNA2
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
Sequence
- Sequence statusComplete
- Length187
- Mass (Da)19,776
- Last updated2006-01-24 v1
- Checksum14ED51EA94F4B56A
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000230 EMBL· GenBank· DDBJ | ABC24393.1 EMBL· GenBank· DDBJ | Genomic DNA |