W9T9W7 · W9T9W7_9PSED
- ProteinMultifunctional fusion protein
- Genelon
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1268 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
function
ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.
Catalytic activity
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 16 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 19 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 38 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 41 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 121-128 | ATP (UniProtKB | ChEBI) | ||||
Sequence: PTGSGKTL | ||||||
Binding site | 822-829 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GPPGVGKT | ||||||
Active site | 1144 | |||||
Sequence: S | ||||||
Active site | 1187 | |||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | ATP-dependent peptidase activity | |
Molecular Function | ATP-dependent protein folding chaperone | |
Molecular Function | protein dimerization activity | |
Molecular Function | sequence-specific DNA binding | |
Molecular Function | serine-type endopeptidase activity | |
Molecular Function | unfolded protein binding | |
Molecular Function | zinc ion binding | |
Biological Process | cellular response to heat | |
Biological Process | protein quality control for misfolded or incompletely synthesized proteins |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameMultifunctional fusion protein
Including 2 domains:
- Recommended nameLon protease
- EC number
- Alternative names
- Recommended nameATP-dependent Clp protease ATP-binding subunit ClpX
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionW9T9W7
Proteomes
Subcellular Location
Expression
Induction
By heat shock.
Interaction
Subunit
Component of the ClpX-ClpP complex. Forms a hexameric ring that, in the presence of ATP, binds to fourteen ClpP subunits assembled into a disk-like structure with a central cavity, resembling the structure of eukaryotic proteasomes.
Homohexamer. Organized in a ring with a central cavity.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 4-57 | ClpX-type ZB | ||||
Sequence: TRNGEDSGKLLYCSFCGKSQHEVRKLIAGPSVFICDECVDLCNDIIREEVQEAQ | ||||||
Domain | 477-670 | Lon N-terminal | ||||
Sequence: LPLLPLRDVVVYPHMVIPLFVGREKSIEALESAMAGDKQILLLAQKNPADDDPVEDALYRVGTVATVLQLLKLPDGTVKVLVEGEQRGVIERFLEVDDHCRAEVALIEESEVEARESEVFTRSLLSQFEQYVQLGKKVPAEVLSSLSSIDEPARLVDTMAAHMALKIEQKQEILEITELPARVEHVLALLDAEI | ||||||
Domain | 1057-1238 | Lon proteolytic | ||||
Sequence: QDQVGQVTGLAWTQVGGELLTIEAAVVPGKGRLTKTGSLGEVMGESITAALTVVRSRATSLGIAVDFHEKQDIHIHVPEGATPKDGPSAGIGMCTALVSALTQIPVRADVAMTGEITLRGQVLAIGGLKEKLLAAHRGGIKTVIIPEENQRDLKEIPENIKQDLQIKPVKWIDEVLQIALQY | ||||||
Region | 1246-1268 | Disordered | ||||
Sequence: AAPEIVAKDDKREPDSKERISTH | ||||||
Compositional bias | 1248-1268 | Basic and acidic residues | ||||
Sequence: PEIVAKDDKREPDSKERISTH |
Sequence similarities
Belongs to the ClpX chaperone family.
Belongs to the peptidase S16 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,268
- Mass (Da)140,527
- Last updated2014-05-14 v1
- Checksum4CB8354A6B187992
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1248-1268 | Basic and acidic residues | ||||
Sequence: PEIVAKDDKREPDSKERISTH |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AZSV01000002 EMBL· GenBank· DDBJ | EXF47248.1 EMBL· GenBank· DDBJ | Genomic DNA |