P9WPE9 · CH601_MYCTU
- ProteinChaperonin GroEL 1
- GenegroEL1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids539 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Prevents aggregation of substrate proteins and promotes their refolding (PubMed:15327959, PubMed:19717599, PubMed:21094166).
In vitro, activity may be independent of the presence or absence of the GroES co-chaperonin or ATP (PubMed:15327959).
Shows weak ATPase activity (PubMed:15327959, PubMed:32812602).
In vitro, activity may be independent of the presence or absence of the GroES co-chaperonin or ATP (PubMed:15327959).
Shows weak ATPase activity (PubMed:15327959, PubMed:32812602).
Involved in copper homeostasis (PubMed:32808291, PubMed:32812602).
Binds copper and may help maintaining copper homeostasis when copper is present in excess, notably in the macrophage phagosome, by acting as a metal storage protein (PubMed:32808291, PubMed:32812602).
Could be involved in copper resistance during mycobacterial biofilm formation (PubMed:32812602).
Protects from copper stress in vitro (PubMed:32808291).
Can also bind other metals, but binds copper with relatively higher affinity compared to nickel and cobalt (PubMed:32808291).
May play an important role in survival under low aeration by affecting the expression of genes known for hypoxia response (PubMed:26822628).
Binds copper and may help maintaining copper homeostasis when copper is present in excess, notably in the macrophage phagosome, by acting as a metal storage protein (PubMed:32808291, PubMed:32812602).
Could be involved in copper resistance during mycobacterial biofilm formation (PubMed:32812602).
Protects from copper stress in vitro (PubMed:32808291).
Can also bind other metals, but binds copper with relatively higher affinity compared to nickel and cobalt (PubMed:32808291).
May play an important role in survival under low aeration by affecting the expression of genes known for hypoxia response (PubMed:26822628).
Miscellaneous
M.tuberculosis contains two copies of the groEL gene, groEL1 and groEL2. GroEL2 is probably the housekeeping chaperonin, with the GroEL1 proteins having evolved, following an ancestral gene duplication event, to take on a more specialized role or roles.
Recombinant GroEL of M.tuberculosis is unable to act as effective molecular chaperone when expressed in Escherichia coli (PubMed:18227175, PubMed:19717599, PubMed:22834700).
Although M.tuberculosis GroEL1 is capable of oligomerization in its native environment, it cannot do the same in E.coli, which probably explains its lack of chaperone activity in E.coli (PubMed:19717599).
Can complement M.smegmatis mutants (PubMed:22834700).
Although M.tuberculosis GroEL1 is capable of oligomerization in its native environment, it cannot do the same in E.coli, which probably explains its lack of chaperone activity in E.coli (PubMed:19717599).
Can complement M.smegmatis mutants (PubMed:22834700).
Catalytic activity
Activity regulation
Oligomerization, which is mediated by phosphorylation, is required for chaperone activity. Lower oligomeric GroELs possess substrate binding activity but are inefficient in promoting refolding (PubMed:19717599).
The binding of copper protects GroEL1 from destabilization and increases its ATPase activity (PubMed:32812602).
The binding of copper protects GroEL1 from destabilization and increases its ATPase activity (PubMed:32812602).
Kinetics
kcat for ATPase activity is 0.16 min-1.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | bacterial nucleoid | |
Cellular Component | GroEL-GroES complex | |
Cellular Component | peptidoglycan-based cell wall | |
Cellular Component | plasma membrane | |
Molecular Function | ATP binding | |
Molecular Function | ATP-dependent protein folding chaperone | |
Molecular Function | isomerase activity | |
Molecular Function | metal ion binding | |
Molecular Function | single-stranded DNA binding | |
Molecular Function | unfolded protein binding | |
Biological Process | chaperone cofactor-dependent protein refolding | |
Biological Process | DNA protection | |
Biological Process | nucleoid organization | |
Biological Process | positive regulation of transcription regulatory region DNA binding | |
Biological Process | protein refolding | |
Biological Process | response to heat |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameChaperonin GroEL 1
- EC number
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycobacterium > Mycobacterium tuberculosis complex
Accessions
- Primary accessionP9WPE9
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Not essential (PubMed:18227175, PubMed:26822628).
Increased heat sensitivity (at 55 degrees Celsius) (PubMed:18227175).
Inactivation of the gene does not affect cell wall lipids, or growth and survival in macrophages, but mutant shows slower growth in the mouse lung and spleen in early infection and fails to produce granulomatous inflammation in either mice or guinea pigs (PubMed:18227175).
This is associated with reduced cytokine expression in infected animals and macrophages (PubMed:18227175).
Knockout of the gene leads to differential gene expression under low aeration stress, including down regulation of genes in copper response and genes encoding members of folate synthesis super pathway (PubMed:26822628).
Survival under low aeration is significantly compromised in this knockout mutant (PubMed:26822628).
Knockout mutant shows increased sensitivity to Cu2+ (PubMed:32808291).
Increased heat sensitivity (at 55 degrees Celsius) (PubMed:18227175).
Inactivation of the gene does not affect cell wall lipids, or growth and survival in macrophages, but mutant shows slower growth in the mouse lung and spleen in early infection and fails to produce granulomatous inflammation in either mice or guinea pigs (PubMed:18227175).
This is associated with reduced cytokine expression in infected animals and macrophages (PubMed:18227175).
Knockout of the gene leads to differential gene expression under low aeration stress, including down regulation of genes in copper response and genes encoding members of folate synthesis super pathway (PubMed:26822628).
Survival under low aeration is significantly compromised in this knockout mutant (PubMed:26822628).
Knockout mutant shows increased sensitivity to Cu2+ (PubMed:32808291).
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 25 | Lack of phosphorylation by PknF; when associated with A-54. | ||||
Sequence: T → A | ||||||
Mutagenesis | 54 | Lack of phosphorylation by PknF; when associated with A-25. | ||||
Sequence: T → A | ||||||
Natural variant | 467 | in strain: Erdman | ||||
Sequence: N → K | ||||||
Mutagenesis | 522-539 | Cannot bind nickel, cobalt or copper. | ||||
Sequence: Missing |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1 variant from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylserine | ||||
Sequence: S | ||||||
Chain | PRO_0000063451 | 2-539 | Chaperonin GroEL 1 | |||
Sequence: SKLIEYDETARRAMEVGMDKLADTVRVTLGPRGRHVVLAKAFGGPTVTNDGVTVAREIELEDPFEDLGAQLVKSVATKTNDVAGDGTTTATILAQALIKGGLRLVAAGVNPIALGVGIGKAADAVSEALLASATPVSGKTGIAQVATVSSRDEQIGDLVGEAMSKVGHDGVVSVEESSTLGTELEFTEGIGFDKGFLSAYFVTDFDNQQAVLEDALILLHQDKISSLPDLLPLLEKVAGTGKPLLIVAEDVEGEALATLVVNAIRKTLKAVAVKGPYFGDRRKAFLEDLAVVTGGQVVNPDAGMVLREVGLEVLGSARRVVVSKDDTVIVDGGGTAEAVANRAKHLRAEIDKSDSDWDREKLGERLAKLAGGVAVIKVGAATETALKERKESVEDAVAAAKAAVEEGIVPGGGASLIHQARKALTELRASLTGDEVLGVDVFSEALAAPLFWIAANAGLDGSVVVNKVSELPAGHGLNVNTLSYGDLAADGVIDPVKVTRSAVLNASSVARMVLTTETVVVDKPAKAEDHDHHHGHAH | ||||||
Modified residue | 25 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 54 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 393 | Phosphoserine; in tetradecamer | ||||
Sequence: S |
Post-translational modification
Phosphorylated on Thr-25 and Thr-54 by PknF (PubMed:19201798).
Phosphorylated on Ser-393 by an unknown kinase (PubMed:19717599).
Phosphorylated on Ser-393 by an unknown kinase (PubMed:19717599).
N-terminus is acetylated by RimI.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Induction
In response to heat shock (45 degrees Celsius) and hyperosmolarity.
Interaction
Subunit
Forms a cylinder of 14 subunits composed of two heptameric rings stacked back-to-back (Probable). Also exists as lower oligomers, including monomeric, dimeric and heptameric forms (PubMed:15327959, PubMed:19717599, PubMed:32808291, PubMed:32812602).
The switch between the single-ring (heptameric) and double-ring (tetradecameric) forms is mediated by phosphorylation on Ser-393 (PubMed:19717599).
Interacts with the co-chaperonin GroES (By similarity).
The switch between the single-ring (heptameric) and double-ring (tetradecameric) forms is mediated by phosphorylation on Ser-393 (PubMed:19717599).
Interacts with the co-chaperonin GroES (By similarity).
Protein-protein interaction databases
Structure
Family & Domains
Domain
Each subunit is composed of an apical domain, an intermediate domain and an equatorial domain (PubMed:32808291).
The apical domain is sufficient for substrate recognition (PubMed:21094166).
Contains a characteristic histidine-rich C terminus which is essential for copper binding (PubMed:32808291).
Copper binding causes conformational rearrangement (PubMed:32808291).
The apical domain is sufficient for substrate recognition (PubMed:21094166).
Contains a characteristic histidine-rich C terminus which is essential for copper binding (PubMed:32808291).
Copper binding causes conformational rearrangement (PubMed:32808291).
Sequence similarities
Belongs to the chaperonin (HSP60) family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length539
- Mass (Da)55,877
- Last updated2014-04-16 v1
- Checksum3E0B93164C091B63
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X60350 EMBL· GenBank· DDBJ | CAA42909.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL123456 EMBL· GenBank· DDBJ | CCP46239.1 EMBL· GenBank· DDBJ | Genomic DNA |