V6M3Y3 · V6M3Y3_9BACL
- ProteinATP-dependent protease subunit HslV
- GenehslV
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids180 (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 | 7 | ||||
Binding site | 164 | Na+ (UniProtKB | ChEBI) | |||
Binding site | 167 | Na+ (UniProtKB | ChEBI) | |||
Binding site | 170 | 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
Names & Taxonomy
Protein names
- Recommended nameATP-dependent protease subunit HslV
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Paenibacillaceae > Brevibacillus
Accessions
- Primary accessionV6M3Y3
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
- Length180
- Mass (Da)19,597
- Last updated2014-02-19 v1
- ChecksumF0DF2521C85B868A
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AYJU01000017 EMBL· GenBank· DDBJ | EST52570.1 EMBL· GenBank· DDBJ | Genomic DNA |