L7V3Y7 · L7V3Y7_MYCL1
- ProteinChaperonin GroEL
- GenegroEL
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids539 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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 | 478-480 | ATP (UniProtKB | ChEBI) | |||
Binding site | 494 | ATP (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | capsule | |
Cellular Component | cell surface | |
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 > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycobacterium > Mycobacterium ulcerans group
Accessions
- Primary accessionL7V3Y7
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Interaction
Subunit
Forms a cylinder of 14 subunits composed of two heptameric rings stacked back-to-back. Interacts with the co-chaperonin GroES.
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 520-539 | Disordered | |||
Compositional bias | 522-539 | Basic and acidic residues | |||
Sequence similarities
Belongs to the chaperonin (HSP60) family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length539
- Mass (Da)55,858
- Last updated2013-04-03 v1
- MD5 Checksum58418D2E2307FEFD0F4C79340E5AE414
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 522-539 | Basic and acidic residues | |||
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP003899 EMBL· GenBank· DDBJ | AGC61255.1 EMBL· GenBank· DDBJ | Genomic DNA |