A0A1F6YI50 · A0A1F6YI50_9BACT
- ProteinChaperonin GroEL
- GenegroEL
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids548 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
Catalytic activity
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 29-32 | ATP (UniProtKB | ChEBI) | |||
Binding site | 86-90 | ATP (UniProtKB | ChEBI) | |||
Binding site | 416 | ATP (UniProtKB | ChEBI) | |||
Binding site | 485-487 | ATP (UniProtKB | ChEBI) | |||
Binding site | 501 | ATP (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | ATP binding | |
Molecular Function | ATP-dependent protein folding chaperone | |
Molecular Function | isomerase activity | |
Molecular Function | unfolded protein binding | |
Biological Process | protein refolding |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameChaperonin GroEL
- EC number
- Alternative names
Gene names
Organism names
- Taxonomic lineageBacteria > Candidatus Nomurabacteria
Accessions
- Primary accessionA0A1F6YI50
Proteomes
Subcellular Location
Interaction
Subunit
Forms a cylinder of 14 subunits composed of two heptameric rings stacked back-to-back. Interacts with the co-chaperonin GroES.
Structure
Sequence
- Sequence statusComplete
- Length548
- Mass (Da)58,248
- Last updated2017-02-15 v1
- MD5 ChecksumEBD49E3F7BAB91E954AAE199651B8874
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
MFVW01000025 EMBL· GenBank· DDBJ | OGJ06062.1 EMBL· GenBank· DDBJ | Genomic DNA |