A0A5C9T5B7 · A0A5C9T5B7_VIBCL
- ProteinATP-dependent protease subunit HslV
- GenehslV
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids185 (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 | 2 | ||||
Binding site | 157 | Na+ (UniProtKB | ChEBI) | |||
Binding site | 160 | Na+ (UniProtKB | ChEBI) | |||
Binding site | 163 | 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 > Pseudomonadota > Gammaproteobacteria > Vibrionales > Vibrionaceae > Vibrio
Accessions
- Primary accessionA0A5C9T5B7
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.
Structure
Sequence
- Sequence statusComplete
- Length185
- Mass (Da)19,875
- Last updated2021-09-29 v1
- ChecksumCA307BD829234E88
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
VSGZ01000007 EMBL· GenBank· DDBJ | TXY94180.1 EMBL· GenBank· DDBJ | Genomic DNA |