A0AAE3TEK4 · A0AAE3TEK4_9BACT
- ProteinATP-dependent protease subunit HslV
- GenehslV
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids175 (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 | 5 | ||||
Binding site | 160 | Na+ (UniProtKB | ChEBI) | |||
Binding site | 163 | Na+ (UniProtKB | ChEBI) | |||
Binding site | 166 | 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
- Strain
- Taxonomic lineageBacteria > Thermodesulfobacteriota > Thermodesulfobacteria > Thermodesulfobacteriales > Thermodesulfobacteriaceae > Thermodesulfobacterium
Accessions
- Primary accessionA0AAE3TEK4
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
- Length175
- Mass (Da)18,856
- Last updated2024-05-29 v1
- MD5 ChecksumA8BF0DEFD608D7A35D8A5DC35D21930B
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JAPHEG010000006 EMBL· GenBank· DDBJ | MDF2954084.1 EMBL· GenBank· DDBJ | Genomic DNA |