A0A7W4V0A5 · A0A7W4V0A5_9MICO
- ProteinChaperone protein DnaJ
- GenednaJ
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids372 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Cofactor
Note: Binds 2 Zn2+ ions per monomer.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 140 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 143 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 157 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 160 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 183 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 186 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 197 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 200 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | ATP binding | |
Molecular Function | heat shock protein binding | |
Molecular Function | unfolded protein binding | |
Molecular Function | zinc ion binding | |
Biological Process | chaperone cofactor-dependent protein refolding | |
Biological Process | DNA replication | |
Biological Process | protein refolding | |
Biological Process | response to heat |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameChaperone protein DnaJ
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Micrococcales > Microbacteriaceae > Microbacterium
Accessions
- Primary accessionA0A7W4V0A5
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 3-67 | J | ||||
Sequence: DHYEVLGVSREATSDEIKKAYRRLARQLHPDVNPGEDASEKFKLVTHAYDVLSDPEQRRRYDMGG | ||||||
Domain | 127-209 | CR-type | ||||
Sequence: GVHRDLEVDTAVLCQTCEGSCCQPGTSPVTCDICHGSGHVQRTVRSLLGNVVTNQPCATCQGYGTTIPYPCATCQGQGRVRER | ||||||
Zinc finger | 127-209 | CR-type | ||||
Sequence: GVHRDLEVDTAVLCQTCEGSCCQPGTSPVTCDICHGSGHVQRTVRSLLGNVVTNQPCATCQGYGTTIPYPCATCQGQGRVRER |
Domain
The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity.
Sequence similarities
Belongs to the DnaJ family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length372
- Mass (Da)39,918
- Last updated2021-06-02 v1
- Checksum7071A955299DABEF