A0A0D6KM56 · A0A0D6KM56_9CYAN
- ProteinChaperonin GroEL
- GenegroEL
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids546 (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 | 413 | ATP (UniProtKB | ChEBI) | |||
Binding site | 495 | ATP (UniProtKB | ChEBI) | |||
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
- Organism
- Strain
- Taxonomic lineageBacteria > Cyanobacteriota > Cyanophyceae > Nostocales > Tolypothrichaceae > Tolypothrix
Accessions
- Primary accessionA0A0D6KM56
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.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for coiled coil, region.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Coiled coil | 337-364 | ||||
Region | 527-546 | Disordered | |||
Sequence similarities
Belongs to the chaperonin (HSP60) family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length546
- Mass (Da)57,736
- Last updated2015-05-27 v1
- MD5 Checksum81DA600878F9FC359D24A4DDB2EED37C
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AGCR01000051 EMBL· GenBank· DDBJ | EKF00857.1 EMBL· GenBank· DDBJ | Genomic DNA |