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UniProtKB - P0A6F5 (CH60_ECOLI)

Protein

60 kDa chaperonin

Gene

groL

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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

View the complete GO annotation on QuickGO ...

GO - Biological processi

  • 'de novo' protein folding Source: GO_Central
  • cell cycle Source: UniProtKB-KW
  • cell division Source: UniProtKB-KW
  • chaperone cofactor-dependent protein refolding Source: EcoCyc
  • protein folding Source: EcoCyc
  • protein refolding Source: UniProtKB-UniRule
  • response to heat Source: EcoliWiki
  • response to radiation Source: EcoCyc
  • virion assembly Source: EcoliWiki
View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionChaperone
Biological processCell cycle, Cell division
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10599-MONOMER
MetaCyc:EG10599-MONOMER
BRENDAi3.6.4.9 2026
SABIO-RKiP0A6F5

Names & Taxonomyi

Protein namesi
Recommended name:
60 kDa chaperoninUniRule annotation
Alternative name(s):
GroEL proteinUniRule annotation
Protein Cpn60UniRule annotation
Gene namesi
Name:groLUniRule annotation
Synonyms:groELUniRule annotation, mopA
Ordered Locus Names:b4143, JW4103
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10599 groL

Subcellular locationi

GO - Cellular componenti

View the complete GO annotation on QuickGO ...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi2A → S: Complex stability is significantly decreased; when associated with S-76, same residues as in M.tuberculosis. 1 Publication1
Mutagenesisi76E → S: Complex stability is significantly decreased; when associated with S-2, same residues as in M.tuberculosis. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00000633582 – 54860 kDa chaperoninAdd BLAST547

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei34N6-succinyllysine1 Publication1
Modified residuei51N6-succinyllysine1 Publication1
Modified residuei117N6-acetyllysine; alternate1 Publication1
Modified residuei117N6-succinyllysine; alternate1 Publication1
Modified residuei277N6-succinyllysine1 Publication1
Modified residuei321N6-succinyllysine1 Publication1
Modified residuei390N6-succinyllysine1 Publication1

Post-translational modificationi

Phosphorylated reversibly during heat shock.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP0A6F5
PaxDbiP0A6F5
PRIDEiP0A6F5

2D gel databases

SWISS-2DPAGEiP0A6F5

PTM databases

CarbonylDBiP0A6F5
iPTMnetiP0A6F5

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 Publication

Binary interactionsi

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi4263077, 558 interactors
852957, 1 interactor
ComplexPortaliCPX-2113 GroEL-GroES complex
DIPiDIP-339N
IntActiP0A6F5, 700 interactors
MINTiP0A6F5
STRINGi316385.ECDH10B_4336

Structurei

Secondary structure

1548
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP0A6F5
SMRiP0A6F5
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A6F5

Family & Domainsi

Sequence similaritiesi

Belongs to the chaperonin (HSP60) family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CJ9 Bacteria
COG0459 LUCA
HOGENOMiHOG000076290
InParanoidiP0A6F5
KOiK04077
PhylomeDBiP0A6F5

Family and domain databases

CDDicd03344 GroEL, 1 hit
Gene3Di1.10.560.10, 1 hit
3.30.260.10, 1 hit
3.50.7.10, 1 hit
HAMAPiMF_00600 CH60, 1 hit
InterProiView 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
PfamiView protein in Pfam
PF00118 Cpn60_TCP1, 1 hit
PRINTSiPR00298 CHAPERONIN60
SUPFAMiSSF48592 SSF48592, 1 hit
SSF52029 SSF52029, 1 hit
SSF54849 SSF54849, 1 hit
TIGRFAMsiTIGR02348 GroEL, 1 hit
PROSITEiView protein in PROSITE
PS00296 CHAPERONINS_CPN60, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A6F5-1 [UniParc]FASTAAdd to basket
« Hide
        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
Length:548
Mass (Da):57,329
Last modified:January 23, 2007 - v2
Checksum:iCD3A0FB505F74AD1
GO

Sequence cautioni

The sequence AAA23934 differs from that shown. Reason: Frameshift at positions 424 and 455.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti83 – 86DAAG → GALQ in CAA30739 (PubMed:2901493).Curated4
Sequence conflicti262L → A in CAA30698 (PubMed:2897629).Curated1
Sequence conflicti267M → I in CAA30698 (PubMed:2897629).Curated1
Sequence conflicti343Q → R in AAA23934 (PubMed:2578448).Curated1

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.
PIRiS56371 BVECGL
RefSeqiNP_418567.1, NC_000913.3
WP_000729117.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC77103; AAC77103; b4143
BAE78145; BAE78145; BAE78145
GeneIDi948665
KEGGiecj:JW4103
eco:b4143
PATRICifig|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.
PIRiS56371 BVECGL
RefSeqiNP_418567.1, NC_000913.3
WP_000729117.1, NZ_LN832404.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AONX-ray3.00A/B/C/D/E/F/G/H/I/J/K/L/M/N2-548[»]
1DK7X-ray2.02A/B191-336[»]
1DKDX-ray2.10A/B/C/D191-336[»]
1FY9X-ray2.20A191-376[»]
1FYAX-ray2.20A191-376[»]
1GR5electron microscopy7.90A/B/C/D/E/F/G/H/I/J/K/L/M/N2-548[»]
1GRLX-ray2.80A/B/C/D/E/F/G1-548[»]
1GRUelectron microscopy12.50A/B/C/D/E/F/G/H/I/J/K/L/M/N2-548[»]
1JONX-ray2.50A191-345[»]
1KIDX-ray1.70A188-376[»]
1KP8X-ray2.00A/B/C/D/E/F/G/H/I/J/K/L/M/N2-548[»]
1LA1X-ray2.06A188-379[»]
1MNFX-ray3.00A/B/C/D/E/F/G/H/I/J/K/L/M/N2-548[»]
1OELX-ray2.80A/B/C/D/E/F/G2-548[»]
1PCQX-ray2.81A/B/C/D/E/F/G/H/I/J/K/L/M/N2-525[»]
1PF9X-ray2.99A/B/C/D/E/F/G/H/I/J/K/L/M/N2-525[»]
1SS8X-ray2.70A/B/C/D/E/F/G2-525[»]
1SVTX-ray2.81A/B/C/D/E/F/G/H/I/J/K/L/M/N2-525[»]
1SX3X-ray2.00A/B/C/D/E/F/G/H/I/J/K/L/M/N2-526[»]
1SX4X-ray3.00A/B/C/D/E/F/G/H/I/J/K/L/M/N2-525[»]
1XCKX-ray2.92A/B/C/D/E/F/G/H/I/J/K/L/M/N2-548[»]
2C7Celectron microscopy7.70A/B/C/D/E/F/G/H/I/J/K/L/M/N2-548[»]
2C7Delectron microscopy8.70A/B/C/D/E/F/G/H/I/J/K/L/M/N2-548[»]
2C7Eelectron microscopy9.70A/B/C/D/E/F/G/H/I/J/K/L/M/N2-548[»]
2CGTelectron microscopy8.20A/B/C/D/E/F/G/H/I/J/K/L/M/N2-548[»]
2EU1X-ray3.29A/B/C/D/E/F/G/H/I/J/K/L/M/N1-548[»]
2NWCX-ray3.02A/B/C/D/E/F/G/H/I/J/K/L/M/N2-548[»]
2YEYX-ray3.30A/B/C/D/E/F/G/H/I/J/K/L/M/N2-525[»]
3C9Velectron microscopy4.70A/B/C/D/E/F/G/H/I/J/K/L/M/N2-527[»]
3CAUelectron microscopy4.20A/B/C/D/E/F/G/H/I/J/K/L/M/N2-527[»]
3VZ6X-ray1.50A191-376[»]
3VZ7X-ray1.80A191-376[»]
3VZ8X-ray1.90A/B/C191-376[»]
3WVLX-ray3.79A/B/C/D/E/F/G/H/I/J/K/L/M/N1-548[»]
3ZPZelectron microscopy8.90A/B/C/D/E/F/G/H/I/J/K/L/M/N2-527[»]
3ZQ0electron microscopy9.20A/B/C/D/E/F/G/H/I/J/K/L/M/N2-525[»]
3ZQ1electron microscopy15.90A/B/C/D/E/F/G/H/I/J/K/L/M/N2-527[»]
4AAQelectron microscopy8.00A/B/C/D/E/F/G/H/I/J/K/L/M/N1-548[»]
4AARelectron microscopy8.00A/B/C/D/E/F/G/H/I/J/K/L/M/N1-548[»]
4AASelectron microscopy8.50A/B/C/D/E/F/G/H/I/J/K/L/M/N1-548[»]
4AAUelectron microscopy8.50A/B/C/D/E/F/G/H/I/J/K/L/M/N1-548[»]
4AB2electron microscopy8.50A/B/C/D/E/F/G/H/I/J/K/L/M/N1-548[»]
4AB3electron microscopy8.50A/B/C/D/E/F/G/H/I/J/K/L/M/N1-548[»]
4V43X-ray3.521/2/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/Z2-548[»]
4WGLX-ray3.13A/B/C/D/E/F/G/H/I/J/K/L/M/N1-548[»]
4WSCX-ray3.04A/B/C/D/E/F/G/H/I/J/K/L/M/N1-548[»]
5OPWX-ray3.19A/B/C/D/E/F/G/H/I/J/K/L/M/N2-548[»]
5OPXX-ray3.64A/B/C/D/E/F/G/H/I/J/K/L/M/N1-548[»]
5W0Selectron microscopy3.50A/B/C/D/E/F/G/H/I/J/K/L/M/N2-525[»]
ProteinModelPortaliP0A6F5
SMRiP0A6F5
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263077, 558 interactors
852957, 1 interactor
ComplexPortaliCPX-2113 GroEL-GroES complex
DIPiDIP-339N
IntActiP0A6F5, 700 interactors
MINTiP0A6F5
STRINGi316385.ECDH10B_4336

PTM databases

CarbonylDBiP0A6F5
iPTMnetiP0A6F5

2D gel databases

SWISS-2DPAGEiP0A6F5

Proteomic databases

EPDiP0A6F5
PaxDbiP0A6F5
PRIDEiP0A6F5

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77103; AAC77103; b4143
BAE78145; BAE78145; BAE78145
GeneIDi948665
KEGGiecj:JW4103
eco:b4143
PATRICifig|1411691.4.peg.2557

Organism-specific databases

EchoBASEiEB0594
EcoGeneiEG10599 groL

Phylogenomic databases

eggNOGiENOG4105CJ9 Bacteria
COG0459 LUCA
HOGENOMiHOG000076290
InParanoidiP0A6F5
KOiK04077
PhylomeDBiP0A6F5

Enzyme and pathway databases

BioCyciEcoCyc:EG10599-MONOMER
MetaCyc:EG10599-MONOMER
BRENDAi3.6.4.9 2026
SABIO-RKiP0A6F5

Miscellaneous databases

EvolutionaryTraceiP0A6F5
PROiPR:P0A6F5

Family and domain databases

CDDicd03344 GroEL, 1 hit
Gene3Di1.10.560.10, 1 hit
3.30.260.10, 1 hit
3.50.7.10, 1 hit
HAMAPiMF_00600 CH60, 1 hit
InterProiView 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
PfamiView protein in Pfam
PF00118 Cpn60_TCP1, 1 hit
PRINTSiPR00298 CHAPERONIN60
SUPFAMiSSF48592 SSF48592, 1 hit
SSF52029 SSF52029, 1 hit
SSF54849 SSF54849, 1 hit
TIGRFAMsiTIGR02348 GroEL, 1 hit
PROSITEiView protein in PROSITE
PS00296 CHAPERONINS_CPN60, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiCH60_ECOLI
AccessioniPrimary (citable) accession number: P0A6F5
Secondary accession number(s): P06139, Q2M6G1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: November 7, 2018
This is version 143 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
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