A0A5N8YG12 · A0A5N8YG12_9CHLR
- ProteinChaperonin GroEL
- GenegroL
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids539 (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.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | GroEL-GroES complex | |
Molecular Function | ATP binding | |
Molecular Function | ATP-dependent protein folding chaperone | |
Molecular Function | isomerase activity | |
Molecular Function | unfolded protein binding | |
Biological Process | chaperone cofactor-dependent protein refolding | |
Biological Process | protein refolding | |
Biological Process | response to heat |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameChaperonin GroEL
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Chloroflexota > Dehalococcoidia > SAR202 cluster
Accessions
- Primary accessionA0A5N8YG12
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
- Length539
- Mass (Da)57,612
- Last updated2020-04-22 v1
- Checksum6DDE0FA9C4CFE342
Keywords
- Technical term