UniProtKB - P0A6F5 (CH60_ECOLI)
Protein
60 kDa chaperonin
Gene
groL
Organism
Escherichia coli (strain K12)
Status
Functioni
Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
Essential for the growth of the bacteria and the assembly of several bacteriophages. Also plays a role in coupling between replication of the F plasmid and cell division of the cell.
Miscellaneous
This protein shows ATPase activity.
Caution
Was originally designated as the ams protein.1 Publication
GO - Molecular functioni
- ATPase activity Source: EcoCyc
- ATP binding Source: EcoCyc
- identical protein binding Source: EcoCyc
- magnesium ion binding Source: EcoCyc
- unfolded protein binding Source: EcoCyc
GO - Biological processi
- cell cycle Source: UniProtKB-KW
- cell division Source: UniProtKB-KW
- chaperone cofactor-dependent protein refolding Source: EcoCyc
- protein folding Source: EcoCyc
- protein refolding Source: GO_Central
- response to heat Source: EcoliWiki
- response to radiation Source: EcoCyc
- virion assembly Source: EcoliWiki
Keywordsi
Molecular function | Chaperone |
Biological process | Cell cycle, Cell division |
Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
BioCyci | EcoCyc:EG10599-MONOMER MetaCyc:EG10599-MONOMER |
BRENDAi | 3.6.4.9, 2026 |
SABIO-RKi | P0A6F5 |
Names & Taxonomyi
Protein namesi | Recommended name: 60 kDa chaperoninUniRule annotationAlternative name(s): GroEL proteinUniRule annotation Protein Cpn60UniRule annotation |
Gene namesi | Name:groLUniRule annotation Synonyms:groELUniRule annotation, mopA Ordered Locus Names:b4143, JW4103 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm UniRule annotation2 Publications
Note: Uniformly located in the cytoplasm (PubMed:20094032). Exclusively localized in foci, usually near 1 cell pole in mid-to-late exponential phase (PubMed:22380631); polar localization depends on the minCDE operon. Foci form near midcell (Probable).Curated2 Publications
Cytosol
- cytosol Source: EcoCyc
- GroEL-GroES complex Source: EcoCyc
Other locations
- membrane Source: UniProtKB
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 2 | A → S: Complex stability is significantly decreased; when associated with S-76, same residues as in M.tuberculosis. 1 Publication | 1 | |
Mutagenesisi | 76 | E → S: Complex stability is significantly decreased; when associated with S-2, same residues as in M.tuberculosis. 1 Publication | 1 |
Chemistry databases
ChEMBLi | CHEMBL4296299 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed2 Publications | |||
ChainiPRO_0000063358 | 2 – 548 | 60 kDa chaperoninAdd BLAST | 547 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 34 | N6-succinyllysine1 Publication | 1 | |
Modified residuei | 51 | N6-succinyllysine1 Publication | 1 | |
Modified residuei | 117 | N6-acetyllysine; alternate1 Publication | 1 | |
Modified residuei | 117 | N6-succinyllysine; alternate1 Publication | 1 | |
Modified residuei | 277 | N6-succinyllysine1 Publication | 1 | |
Modified residuei | 321 | N6-succinyllysine1 Publication | 1 | |
Modified residuei | 390 | N6-succinyllysine1 Publication | 1 |
Post-translational modificationi
Phosphorylated reversibly during heat shock.1 Publication
Keywords - PTMi
Acetylation, PhosphoproteinProteomic databases
jPOSTi | P0A6F5 |
PaxDbi | P0A6F5 |
PRIDEi | P0A6F5 |
2D gel databases
SWISS-2DPAGEi | P0A6F5 |
PTM databases
CarbonylDBi | P0A6F5 |
iPTMneti | P0A6F5 |
MetOSitei | P0A6F5 |
Interactioni
Subunit structurei
Oligomer of 14 subunits composed of two stacked rings of 7 subunits. Complex can be destablized when Ala-2 and Glu-76 are mutated to match these residues in M.tuberculosis (PubMed:15327959).
1 PublicationBinary interactionsi
Hide detailsP0A6F5
GO - Molecular functioni
- identical protein binding Source: EcoCyc
- unfolded protein binding Source: EcoCyc
Protein-protein interaction databases
BioGRIDi | 4263077, 558 interactors 852957, 7 interactors |
ComplexPortali | CPX-2113, GroEL-GroES complex |
DIPi | DIP-339N |
IntActi | P0A6F5, 700 interactors |
MINTi | P0A6F5 |
STRINGi | 511145.b4143 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P0A6F5 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0A6F5 |
Family & Domainsi
Sequence similaritiesi
Belongs to the chaperonin (HSP60) family.UniRule annotation
Phylogenomic databases
eggNOGi | COG0459, Bacteria |
HOGENOMi | CLU_016503_3_0_6 |
InParanoidi | P0A6F5 |
PhylomeDBi | P0A6F5 |
Family and domain databases
CDDi | cd03344, GroEL, 1 hit |
Gene3Di | 1.10.560.10, 1 hit 3.30.260.10, 1 hit 3.50.7.10, 1 hit |
HAMAPi | MF_00600, CH60, 1 hit |
InterProi | View protein in InterPro IPR018370, Chaperonin_Cpn60_CS IPR001844, Chaprnin_Cpn60 IPR002423, Cpn60/TCP-1 IPR027409, GroEL-like_apical_dom_sf IPR027413, GROEL-like_equatorial_sf IPR027410, TCP-1-like_intermed_sf |
Pfami | View protein in Pfam PF00118, Cpn60_TCP1, 1 hit |
PRINTSi | PR00298, CHAPERONIN60 |
SUPFAMi | SSF48592, SSF48592, 1 hit SSF52029, SSF52029, 1 hit SSF54849, SSF54849, 1 hit |
TIGRFAMsi | TIGR02348, GroEL, 1 hit |
PROSITEi | View protein in PROSITE PS00296, CHAPERONINS_CPN60, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P0A6F5-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MAAKDVKFGN DARVKMLRGV NVLADAVKVT LGPKGRNVVL DKSFGAPTIT
60 70 80 90 100
KDGVSVAREI ELEDKFENMG AQMVKEVASK ANDAAGDGTT TATVLAQAII
110 120 130 140 150
TEGLKAVAAG MNPMDLKRGI DKAVTAAVEE LKALSVPCSD SKAIAQVGTI
160 170 180 190 200
SANSDETVGK LIAEAMDKVG KEGVITVEDG TGLQDELDVV EGMQFDRGYL
210 220 230 240 250
SPYFINKPET GAVELESPFI LLADKKISNI REMLPVLEAV AKAGKPLLII
260 270 280 290 300
AEDVEGEALA TLVVNTMRGI VKVAAVKAPG FGDRRKAMLQ DIATLTGGTV
310 320 330 340 350
ISEEIGMELE KATLEDLGQA KRVVINKDTT TIIDGVGEEA AIQGRVAQIR
360 370 380 390 400
QQIEEATSDY DREKLQERVA KLAGGVAVIK VGAATEVEMK EKKARVEDAL
410 420 430 440 450
HATRAAVEEG VVAGGGVALI RVASKLADLR GQNEDQNVGI KVALRAMEAP
460 470 480 490 500
LRQIVLNCGE EPSVVANTVK GGDGNYGYNA ATEEYGNMID MGILDPTKVT
510 520 530 540
RSALQYAASV AGLMITTECM VTDLPKNDAA DLGAAGGMGG MGGMGGMM
Sequence cautioni
The sequence AAA23934 differs from that shown. Reason: Frameshift.Curated
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 83 – 86 | DAAG → GALQ in CAA30739 (PubMed:2901493).Curated | 4 | |
Sequence conflicti | 262 | L → A in CAA30698 (PubMed:2897629).Curated | 1 | |
Sequence conflicti | 267 | M → I in CAA30698 (PubMed:2897629).Curated | 1 | |
Sequence conflicti | 343 | Q → R in AAA23934 (PubMed:2578448).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X07850 Genomic DNA Translation: CAA30698.1 U14003 Genomic DNA Translation: AAA97042.1 U00096 Genomic DNA Translation: AAC77103.1 AP009048 Genomic DNA Translation: BAE78145.1 X07899 Genomic DNA Translation: CAA30739.1 M11294 Genomic DNA Translation: AAA23934.1 Frameshift. |
PIRi | S56371, BVECGL |
RefSeqi | NP_418567.1, NC_000913.3 WP_000729117.1, NZ_STEB01000014.1 |
Genome annotation databases
EnsemblBacteriai | AAC77103; AAC77103; b4143 BAE78145; BAE78145; BAE78145 |
GeneIDi | 58460965 948665 |
KEGGi | ecj:JW4103 eco:b4143 |
PATRICi | fig|1411691.4.peg.2557 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X07850 Genomic DNA Translation: CAA30698.1 U14003 Genomic DNA Translation: AAA97042.1 U00096 Genomic DNA Translation: AAC77103.1 AP009048 Genomic DNA Translation: BAE78145.1 X07899 Genomic DNA Translation: CAA30739.1 M11294 Genomic DNA Translation: AAA23934.1 Frameshift. |
PIRi | S56371, BVECGL |
RefSeqi | NP_418567.1, NC_000913.3 WP_000729117.1, NZ_STEB01000014.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1AON | X-ray | 3.00 | A/B/C/D/E/F/G/H/I/J/K/L/M/N | 2-548 | [»] | |
1DK7 | X-ray | 2.02 | A/B | 191-336 | [»] | |
1DKD | X-ray | 2.10 | A/B/C/D | 191-336 | [»] | |
1FY9 | X-ray | 2.20 | A | 191-376 | [»] | |
1FYA | X-ray | 2.20 | A | 191-376 | [»] | |
1GR5 | electron microscopy | 7.90 | A/B/C/D/E/F/G/H/I/J/K/L/M/N | 2-548 | [»] | |
1GRL | X-ray | 2.80 | A/B/C/D/E/F/G | 1-548 | [»] | |
1GRU | electron microscopy | 12.50 | A/B/C/D/E/F/G/H/I/J/K/L/M/N | 2-548 | [»] | |
1JON | X-ray | 2.50 | A | 191-345 | [»] | |
1KID | X-ray | 1.70 | A | 188-376 | [»] | |
1KP8 | X-ray | 2.00 | A/B/C/D/E/F/G/H/I/J/K/L/M/N | 2-548 | [»] | |
1LA1 | X-ray | 2.06 | A | 188-379 | [»] | |
1MNF | X-ray | 3.00 | A/B/C/D/E/F/G/H/I/J/K/L/M/N | 2-548 | [»] | |
1OEL | X-ray | 2.80 | A/B/C/D/E/F/G | 2-548 | [»] | |
1PCQ | X-ray | 2.81 | A/B/C/D/E/F/G/H/I/J/K/L/M/N | 2-525 | [»] | |
1PF9 | X-ray | 2.99 | A/B/C/D/E/F/G/H/I/J/K/L/M/N | 2-525 | [»] | |
1SS8 | X-ray | 2.70 | A/B/C/D/E/F/G | 2-525 | [»] | |
1SVT | X-ray | 2.81 | A/B/C/D/E/F/G/H/I/J/K/L/M/N | 2-525 | [»] | |
1SX3 | X-ray | 2.00 | A/B/C/D/E/F/G/H/I/J/K/L/M/N | 2-526 | [»] | |
1SX4 | X-ray | 3.00 | A/B/C/D/E/F/G/H/I/J/K/L/M/N | 2-525 | [»] | |
1XCK | X-ray | 2.92 | A/B/C/D/E/F/G/H/I/J/K/L/M/N | 2-548 | [»] | |
2C7C | electron microscopy | 7.70 | A/B/C/D/E/F/G/H/I/J/K/L/M/N | 2-548 | [»] | |
2C7D | electron microscopy | 8.70 | A/B/C/D/E/F/G/H/I/J/K/L/M/N | 2-548 | [»] | |
2C7E | electron microscopy | 9.70 | A/B/C/D/E/F/G/H/I/J/K/L/M/N | 2-548 | [»] | |
2CGT | electron microscopy | 8.20 | A/B/C/D/E/F/G/H/I/J/K/L/M/N | 2-548 | [»] | |
2EU1 | X-ray | 3.29 | A/B/C/D/E/F/G/H/I/J/K/L/M/N | 1-548 | [»] | |
2NWC | X-ray | 3.02 | A/B/C/D/E/F/G/H/I/J/K/L/M/N | 2-548 | [»] | |
2YEY | X-ray | 3.30 | A/B/C/D/E/F/G/H/I/J/K/L/M/N | 2-525 | [»] | |
3C9V | electron microscopy | 4.70 | A/B/C/D/E/F/G/H/I/J/K/L/M/N | 2-527 | [»] | |
3CAU | electron microscopy | 4.20 | A/B/C/D/E/F/G/H/I/J/K/L/M/N | 2-527 | [»] | |
3VZ6 | X-ray | 1.50 | A | 191-376 | [»] | |
3VZ7 | X-ray | 1.80 | A | 191-376 | [»] | |
3VZ8 | X-ray | 1.90 | A/B/C | 191-376 | [»] | |
3WVL | X-ray | 3.79 | A/B/C/D/E/F/G/H/I/J/K/L/M/N | 1-548 | [»] | |
3ZPZ | electron microscopy | 8.90 | A/B/C/D/E/F/G/H/I/J/K/L/M/N | 2-527 | [»] | |
3ZQ0 | electron microscopy | 9.20 | A/B/C/D/E/F/G/H/I/J/K/L/M/N | 2-525 | [»] | |
3ZQ1 | electron microscopy | 15.90 | A/B/C/D/E/F/G/H/I/J/K/L/M/N | 2-527 | [»] | |
4AAQ | electron microscopy | 8.00 | A/B/C/D/E/F/G/H/I/J/K/L/M/N | 1-548 | [»] | |
4AAR | electron microscopy | 8.00 | A/B/C/D/E/F/G/H/I/J/K/L/M/N | 1-548 | [»] | |
4AAS | electron microscopy | 8.50 | A/B/C/D/E/F/G/H/I/J/K/L/M/N | 1-548 | [»] | |
4AAU | electron microscopy | 8.50 | A/B/C/D/E/F/G/H/I/J/K/L/M/N | 1-548 | [»] | |
4AB2 | electron microscopy | 8.50 | A/B/C/D/E/F/G/H/I/J/K/L/M/N | 1-548 | [»] | |
4AB3 | electron microscopy | 8.50 | A/B/C/D/E/F/G/H/I/J/K/L/M/N | 1-548 | [»] | |
4V43 | X-ray | 3.52 | 1/2/A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z | 2-548 | [»] | |
4WGL | X-ray | 3.13 | A/B/C/D/E/F/G/H/I/J/K/L/M/N | 1-548 | [»] | |
4WSC | X-ray | 3.04 | A/B/C/D/E/F/G/H/I/J/K/L/M/N | 1-548 | [»] | |
5OPW | X-ray | 3.19 | A/B/C/D/E/F/G/H/I/J/K/L/M/N | 2-548 | [»] | |
5OPX | X-ray | 3.64 | A/B/C/D/E/F/G/H/I/J/K/L/M/N | 1-548 | [»] | |
5W0S | electron microscopy | 3.50 | A/B/C/D/E/F/G/H/I/J/K/L/M/N | 2-525 | [»] | |
SMRi | P0A6F5 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4263077, 558 interactors 852957, 7 interactors |
ComplexPortali | CPX-2113, GroEL-GroES complex |
DIPi | DIP-339N |
IntActi | P0A6F5, 700 interactors |
MINTi | P0A6F5 |
STRINGi | 511145.b4143 |
Chemistry databases
ChEMBLi | CHEMBL4296299 |
PTM databases
CarbonylDBi | P0A6F5 |
iPTMneti | P0A6F5 |
MetOSitei | P0A6F5 |
2D gel databases
SWISS-2DPAGEi | P0A6F5 |
Proteomic databases
jPOSTi | P0A6F5 |
PaxDbi | P0A6F5 |
PRIDEi | P0A6F5 |
Genome annotation databases
EnsemblBacteriai | AAC77103; AAC77103; b4143 BAE78145; BAE78145; BAE78145 |
GeneIDi | 58460965 948665 |
KEGGi | ecj:JW4103 eco:b4143 |
PATRICi | fig|1411691.4.peg.2557 |
Organism-specific databases
EchoBASEi | EB0594 |
Phylogenomic databases
eggNOGi | COG0459, Bacteria |
HOGENOMi | CLU_016503_3_0_6 |
InParanoidi | P0A6F5 |
PhylomeDBi | P0A6F5 |
Enzyme and pathway databases
BioCyci | EcoCyc:EG10599-MONOMER MetaCyc:EG10599-MONOMER |
BRENDAi | 3.6.4.9, 2026 |
SABIO-RKi | P0A6F5 |
Miscellaneous databases
EvolutionaryTracei | P0A6F5 |
PROi | PR:P0A6F5 |
Family and domain databases
CDDi | cd03344, GroEL, 1 hit |
Gene3Di | 1.10.560.10, 1 hit 3.30.260.10, 1 hit 3.50.7.10, 1 hit |
HAMAPi | MF_00600, CH60, 1 hit |
InterProi | View protein in InterPro IPR018370, Chaperonin_Cpn60_CS IPR001844, Chaprnin_Cpn60 IPR002423, Cpn60/TCP-1 IPR027409, GroEL-like_apical_dom_sf IPR027413, GROEL-like_equatorial_sf IPR027410, TCP-1-like_intermed_sf |
Pfami | View protein in Pfam PF00118, Cpn60_TCP1, 1 hit |
PRINTSi | PR00298, CHAPERONIN60 |
SUPFAMi | SSF48592, SSF48592, 1 hit SSF52029, SSF52029, 1 hit SSF54849, SSF54849, 1 hit |
TIGRFAMsi | TIGR02348, GroEL, 1 hit |
PROSITEi | View protein in PROSITE PS00296, CHAPERONINS_CPN60, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | CH60_ECOLI | |
Accessioni | P0A6F5Primary (citable) accession number: P0A6F5 Secondary accession number(s): P06139, Q2M6G1 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | January 1, 1988 |
Last sequence update: | January 23, 2007 | |
Last modified: | April 7, 2021 | |
This is version 161 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families