P0A7B8 · HSLV_ECOLI
- ProteinATP-dependent protease subunit HslV
- GenehslV
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids176 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. The complex has been shown to be involved in the specific degradation of heat shock induced transcription factors such as RpoH and SulA. In addition, small hydrophobic peptides are also hydrolyzed by HslV. HslV has weak protease activity even in the absence of HslU, but this activity is induced more than 100-fold in the presence of HslU. HslU recognizes protein substrates and unfolds these before guiding them to HslV for hydrolysis. HslV is not believed to degrade folded proteins.
Catalytic activity
Activity regulation
Allosterically activated by HslU binding.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
5.2 μM | Arc-MYL-st11 | 37 |
Arc is a repressor protein, Arc-MYL-st11 is a hyperstable variant of Arc.
Temperature Dependence
Optimum temperature is 55 degrees Celsius.
Features
Showing features for active site, binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | HslUV protease complex | |
Cellular Component | proteasome core complex | |
Molecular Function | ATP binding | |
Molecular Function | identical protein binding | |
Molecular Function | magnesium ion binding | |
Molecular Function | protein domain specific binding | |
Molecular Function | threonine-type endopeptidase activity | |
Biological Process | cellular response to heat | |
Biological Process | protein denaturation | |
Biological Process | proteolysis | |
Biological Process | proteolysis involved in protein catabolic process | |
Biological Process | response to heat |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameATP-dependent protease subunit HslV
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP0A7B8
- Secondary accessions
Proteomes
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 2 | 80% reduced protease activity in the absence of HslU. Almost no effect in the presence of HslU. | ||||
Sequence: T → S | ||||||
Mutagenesis | 2 | No protease activity. | ||||
Sequence: T → V | ||||||
Mutagenesis | 3 | 80% reduced protease activity. | ||||
Sequence: T → S or V | ||||||
Mutagenesis | 6 | No effect. | ||||
Sequence: S → A | ||||||
Mutagenesis | 104 | 50% reduced protease activity. | ||||
Sequence: S → A | ||||||
Mutagenesis | 125 | Almost no protease activity. | ||||
Sequence: S → A | ||||||
Mutagenesis | 144 | No effect. | ||||
Sequence: S → A | ||||||
Mutagenesis | 160 | No protease activity. Cannot form complexes with HslU. | ||||
Sequence: C → A or S | ||||||
Mutagenesis | 173 | Almost no protease activity. | ||||
Sequence: S → A |
PTM/Processing
Features
Showing features for initiator methionine, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000148105 | 2-176 | ATP-dependent protease subunit HslV | |||
Sequence: TTIVSVRRNGHVVIAGDGQATLGNTVMKGNVKKVRRLYNDKVIAGFAGGTADAFTLFELFERKLEMHQGHLVKAAVELAKDWRTDRMLRKLEALLAVADETASLIITGNGDVVQPENDLIAIGSGGPYAQAAARALLENTELSAREIAEKALDIAGDICIYTNHFHTIEELSYKA |
Proteomic databases
Expression
Induction
By heat shock.
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.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P0A7B8 | hslU P0A6H5 | 16 | EBI-552265, EBI-369317 | |
BINARY | P0A7B8 | hslV P0A7B8 | 6 | EBI-552265, EBI-552265 |
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length176
- Mass (Da)19,093
- Last updated2007-01-23 v2
- Checksum3B35E01F51486965
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L19201 EMBL· GenBank· DDBJ | AAB03064.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U00096 EMBL· GenBank· DDBJ | AAC76914.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAE77378.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
D89965 EMBL· GenBank· DDBJ | BAA14040.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
L14281 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |