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P0A6F5

- CH60_ECOLI

UniProt

P0A6F5 - CH60_ECOLI

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Protein
60 kDa chaperonin
Gene
groL, groEL, mopA, b4143, JW4103
Organism
Escherichia coli (strain K12)
Status
Reviewed - - Experimental evidence at protein leveli

Functioni

Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.UniRule annotation
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.UniRule annotation

GO - Molecular functioni

  1. ATP bindingInferred from direct assayi PubMed 9285585 Source: EcoCyc
  2. ATPase activityInferred from direct assayi PubMed 379350 Source: EcoCyc
  3. identical protein bindingInferred from physical interactioni PubMed 16858726PubMed 22575645PubMed 8618836PubMed 9878052 Source: IntAct
  4. protein bindingInferred from physical interactioni PubMed 10077571PubMed 11779463PubMed 12071968PubMed 14517228PubMed 15313620PubMed 15690043PubMed 16239229PubMed 16606699PubMed 16977315PubMed 18394994PubMed 18418386PubMed 20959808PubMed 23746846PubMed 24561554PubMed 8618836PubMed 9285585PubMed 9878052 Source: IntAct
  5. unfolded protein bindingInferred from mutant phenotypei PubMed 2573517 Source: EcoCyc
Complete GO annotation...

GO - Biological processi

  1. ATP catabolic processInferred from direct assayi PubMed 379350 Source: GOC
  2. cell cycleInferred from electronic annotationi Source: UniProtKB-KW
  3. cell divisionInferred from electronic annotationi Source: UniProtKB-KW
  4. protein foldingInferred from mutant phenotypei PubMed 2573517 Source: EcoCyc
  5. protein refoldingInferred from electronic annotationi Source: UniProtKB-HAMAP
  6. response to heatInferred from expression patterni PubMed 8349564 Source: EcoliWiki
  7. virion assemblyInferred from mutant phenotypei PubMed 7015340 Source: EcoliWiki
  1. ATPase activityInferred from direct assayi PubMed 379350 Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Cell cycle, Cell division

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10599-MONOMER.
ECOL316407:JW4103-MONOMER.
SABIO-RKiP0A6F5.

Names & Taxonomyi

Protein namesi
Recommended name:
60 kDa chaperonin
Alternative name(s):
GroEL protein
Protein Cpn60
Gene namesi
Name:groL
Synonyms:groEL, mopA
Ordered Locus Names:b4143, JW4103
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10599. groL.

Subcellular locationi

Cytoplasm
Note: Uniformly located in the cytoplasm (1 Publication). Exclusively localized in foci, usually near 1 cell pole in mid-to-late exponential phase (1 Publication); polar localization depends on the minCDE operon. Foci form near midcell Inferred.2 Publications

GO - Cellular componenti

  1. cytosolInferred from direct assayi PubMed 16858726 Source: UniProtKB
  2. membraneInferred from direct assayi PubMed 16858726 Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 54854760 kDa chaperoninUniRule annotation
PRO_0000063358

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Modified residuei34 – 341N6-succinyllysine1 Publication
Modified residuei51 – 511N6-succinyllysine1 Publication
Modified residuei117 – 1171N6-acetyllysine; alternate1 Publication
Modified residuei117 – 1171N6-succinyllysine; alternate1 Publication
Modified residuei277 – 2771N6-succinyllysine1 Publication
Modified residuei321 – 3211N6-succinyllysine1 Publication
Modified residuei390 – 3901N6-succinyllysine1 Publication

Post-translational modificationi

Phosphorylated reversibly during heat shock.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP0A6F5.
PRIDEiP0A6F5.

2D gel databases

SWISS-2DPAGEiP0A6F5.

Expressioni

Gene expression databases

GenevestigatoriP0A6F5.

Interactioni

Subunit structurei

Oligomer of 14 subunits composed of two stacked rings of 7 subunits.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself7EBI-543750,EBI-543750
aceEP0AFG82EBI-543750,EBI-542683
ACT1P600105EBI-543750,EBI-2169From a different organism.
aroHP008873EBI-543750,EBI-1125143
choP762132EBI-543750,EBI-545155
fhlAP193232EBI-543750,EBI-1113147
groSP0A6F925EBI-543750,EBI-369169
hyfGP773293EBI-543750,EBI-548413
malEP0AEX93EBI-543750,EBI-369910
metKP0A8172EBI-543750,EBI-546295
mlaFP633863EBI-543750,EBI-561408
recFP0A7H03EBI-543750,EBI-556839
rfbCP377452EBI-543750,EBI-557071
TSTP005862EBI-543750,EBI-7900146From a different organism.
ulaRP0A9W03EBI-543750,EBI-560926
uspGP391774EBI-543750,EBI-561722
ybbLP772792EBI-543750,EBI-560090
yhbUP455273EBI-543750,EBI-561157
yhjBP376403EBI-543750,EBI-542016
ypdFP765242EBI-543750,EBI-1128711

Protein-protein interaction databases

BioGridi852957. 1 interaction.
DIPiDIP-339N.
IntActiP0A6F5. 697 interactions.
MINTiMINT-5232496.
STRINGi511145.b4143.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Beta strandi4 – 85
Helixi9 – 2820
Beta strandi37 – 404
Beta strandi43 – 464
Beta strandi48 – 503
Helixi53 – 597
Helixi65 – 8521
Helixi89 – 10820
Helixi113 – 13422
Helixi141 – 15111
Turni152 – 1543
Helixi156 – 16914
Beta strandi173 – 1786
Beta strandi181 – 1844
Beta strandi186 – 1916
Beta strandi193 – 1964
Beta strandi199 – 2013
Helixi202 – 2043
Turni208 – 2114
Beta strandi212 – 2176
Beta strandi219 – 2279
Helixi230 – 2334
Helixi234 – 24310
Beta strandi247 – 2548
Helixi256 – 26712
Beta strandi268 – 2703
Beta strandi273 – 2775
Beta strandi279 – 2813
Helixi282 – 29615
Beta strandi300 – 3023
Helixi303 – 3053
Helixi309 – 3113
Helixi314 – 3163
Beta strandi317 – 3259
Beta strandi330 – 3356
Helixi339 – 35517
Helixi359 – 37517
Beta strandi376 – 3805
Helixi386 – 40924
Beta strandi411 – 4133
Turni414 – 4163
Helixi417 – 4259
Turni426 – 4283
Helixi434 – 44613
Helixi449 – 4579
Helixi462 – 47110
Beta strandi476 – 4794
Turni480 – 4834
Beta strandi484 – 4874
Turni488 – 4925
Beta strandi494 – 4963
Helixi497 – 51519
Beta strandi517 – 5237

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
1J4ZX-ray3.52A/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[»]
1KPOX-ray3.521/2/O/P/Q/R/S/T/U/V/W/X/Y/Z2-548[»]
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[»]
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[»]
ProteinModelPortaliP0A6F5.

Miscellaneous databases

EvolutionaryTraceiP0A6F5.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0459.
HOGENOMiHOG000076290.
KOiK04077.
OMAiVLFGNDA.
OrthoDBiEOG6JDWBZ.
PhylomeDBiP0A6F5.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.50.7.10. 1 hit.
HAMAPiMF_00600. CH60.
InterProiIPR018370. Chaperonin_Cpn60_CS.
IPR001844. Chaprnin_Cpn60.
IPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
IPR027413. GROEL-like_equatorial.
[Graphical view]
PANTHERiPTHR11353. PTHR11353. 1 hit.
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00298. CHAPERONIN60.
SUPFAMiSSF48592. SSF48592. 2 hits.
SSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02348. GroEL. 1 hit.
PROSITEiPS00296. CHAPERONINS_CPN60. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0A6F5-1 [UniParc]FASTA

« Hide

MAAKDVKFGN DARVKMLRGV NVLADAVKVT LGPKGRNVVL DKSFGAPTIT    50
KDGVSVAREI ELEDKFENMG AQMVKEVASK ANDAAGDGTT TATVLAQAII 100
TEGLKAVAAG MNPMDLKRGI DKAVTAAVEE LKALSVPCSD SKAIAQVGTI 150
SANSDETVGK LIAEAMDKVG KEGVITVEDG TGLQDELDVV EGMQFDRGYL 200
SPYFINKPET GAVELESPFI LLADKKISNI REMLPVLEAV AKAGKPLLII 250
AEDVEGEALA TLVVNTMRGI VKVAAVKAPG FGDRRKAMLQ DIATLTGGTV 300
ISEEIGMELE KATLEDLGQA KRVVINKDTT TIIDGVGEEA AIQGRVAQIR 350
QQIEEATSDY DREKLQERVA KLAGGVAVIK VGAATEVEMK EKKARVEDAL 400
HATRAAVEEG VVAGGGVALI RVASKLADLR GQNEDQNVGI KVALRAMEAP 450
LRQIVLNCGE EPSVVANTVK GGDGNYGYNA ATEEYGNMID MGILDPTKVT 500
RSALQYAASV AGLMITTECM VTDLPKNDAA DLGAAGGMGG MGGMGGMM 548
Length:548
Mass (Da):57,329
Last modified:January 23, 2007 - v2
Checksum:iCD3A0FB505F74AD1
GO

Sequence cautioni

The sequence AAA23934.1 differs from that shown. Reason: Frameshift at positions 424 and 455.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Sequence conflicti83 – 864DAAG → GALQ in CAA30739. 1 Publication
Sequence conflicti262 – 2621L → A in CAA30698. 1 Publication
Sequence conflicti267 – 2671M → I in CAA30698. 1 Publication
Sequence conflicti343 – 3431Q → R in AAA23934. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
PIRiBVECGL. S56371.
RefSeqiNP_418567.1. NC_000913.3.
YP_492286.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC77103; AAC77103; b4143.
BAE78145; BAE78145; BAE78145.
GeneIDi12934083.
948665.
KEGGiecj:Y75_p4030.
eco:b4143.
PATRICi32123855. VBIEscCol129921_4275.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 BVECGL. S56371.
RefSeqi NP_418567.1. NC_000913.3.
YP_492286.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
1J4Z X-ray 3.52 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 [» ]
1KPO X-ray 3.52 1/2/O/P/Q/R/S/T/U/V/W/X/Y/Z 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 [» ]
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 [» ]
ProteinModelPortali P0A6F5.
ModBasei Search...

Protein-protein interaction databases

BioGridi 852957. 1 interaction.
DIPi DIP-339N.
IntActi P0A6F5. 697 interactions.
MINTi MINT-5232496.
STRINGi 511145.b4143.

2D gel databases

SWISS-2DPAGEi P0A6F5.

Proteomic databases

PaxDbi P0A6F5.
PRIDEi P0A6F5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC77103 ; AAC77103 ; b4143 .
BAE78145 ; BAE78145 ; BAE78145 .
GeneIDi 12934083.
948665.
KEGGi ecj:Y75_p4030.
eco:b4143.
PATRICi 32123855. VBIEscCol129921_4275.

Organism-specific databases

EchoBASEi EB0594.
EcoGenei EG10599. groL.

Phylogenomic databases

eggNOGi COG0459.
HOGENOMi HOG000076290.
KOi K04077.
OMAi VLFGNDA.
OrthoDBi EOG6JDWBZ.
PhylomeDBi P0A6F5.

Enzyme and pathway databases

BioCyci EcoCyc:EG10599-MONOMER.
ECOL316407:JW4103-MONOMER.
SABIO-RKi P0A6F5.

Miscellaneous databases

EvolutionaryTracei P0A6F5.
PROi P0A6F5.

Gene expression databases

Genevestigatori P0A6F5.

Family and domain databases

Gene3Di 1.10.560.10. 2 hits.
3.50.7.10. 1 hit.
HAMAPi MF_00600. CH60.
InterProi IPR018370. Chaperonin_Cpn60_CS.
IPR001844. Chaprnin_Cpn60.
IPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
IPR027413. GROEL-like_equatorial.
[Graphical view ]
PANTHERi PTHR11353. PTHR11353. 1 hit.
Pfami PF00118. Cpn60_TCP1. 1 hit.
[Graphical view ]
PRINTSi PR00298. CHAPERONIN60.
SUPFAMi SSF48592. SSF48592. 2 hits.
SSF52029. SSF52029. 1 hit.
TIGRFAMsi TIGR02348. GroEL. 1 hit.
PROSITEi PS00296. CHAPERONINS_CPN60. 1 hit.
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Publicationsi

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  1. "Homologous plant and bacterial proteins chaperone oligomeric protein assembly."
    Hemmingsen S.M., Woolford C., van der Vies S.M., Tilly K., Dennis D.T., Georgopoulos C., Hendrix R.W., Ellis R.J.
    Nature 333:330-334(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
    Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
    Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "The complete genome sequence of Escherichia coli K-12."
    Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
    Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Control of cell division by sex factor F in Escherichia coli. III. Participation of the groES (mopB) gene of the host bacteria."
    Miki T., Orita T., Furuno M., Horiuchi T.
    J. Mol. Biol. 201:327-338(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-86.
  6. "Cloning, sequence analysis, and expression of alteration of the mRNA stability gene (ams+) of Escherichia coli."
    Chanda P.K., Ono M., Kuwano M., Kung H.-F.
    J. Bacteriol. 161:446-449(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 298-495.
  7. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-22.
    Strain: K12 / EMG2.
  8. Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.
    Submitted (FEB-1996) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-12.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  9. "A role of RnlA in the RNase LS activity from Escherichia coli."
    Otsuka Y., Koga M., Iwamoto A., Yonesaki T.
    Genes Genet. Syst. 82:291-299(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 4-10.
    Strain: K12.
  10. "The reaction of GroEL (cpn 60) with the ATP analogue 2',3' dialdehyde ATP."
    Thomson G.J., Coggins J.R., Price N.C.
    FEBS Lett. 336:19-22(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 455-519.
  11. "Heat shock in Escherichia coli alters the protein-binding properties of the chaperonin groEL by inducing its phosphorylation."
    Sherman M.Y., Goldberg A.L.
    Nature 357:167-169(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION.
  12. "Residues in chaperonin GroEL required for polypeptide binding and release."
    Fenton W.A., Kashi Y., Furtak K., Horwich A.L.
    Nature 371:614-619(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  13. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  14. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
    Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
    Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-117, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
  15. "Quantitative and spatio-temporal features of protein aggregation in Escherichia coli and consequences on protein quality control and cellular ageing."
    Winkler J., Seybert A., Konig L., Pruggnaller S., Haselmann U., Sourjik V., Weiss M., Frangakis A.S., Mogk A., Bukau B.
    EMBO J. 29:910-923(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  16. "Identification of lysine succinylation as a new post-translational modification."
    Zhang Z., Tan M., Xie Z., Dai L., Chen Y., Zhao Y.
    Nat. Chem. Biol. 7:58-63(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION AT LYS-34; LYS-51; LYS-117; LYS-277; LYS-321 AND LYS-390.
    Strain: K12.
  17. "Isolation and identification of new inner membrane-associated proteins that localize to cell poles in Escherichia coli."
    Li G., Young K.D.
    Mol. Microbiol. 84:276-295(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
    Strain: K12 / MG1655 / ATCC 47076.
  18. "The crystal structure of the bacterial chaperonin GroEL at 2.8 A."
    Braig K., Otwinowski Z., Hegde R.S., Boisvert D.C., Joachimiak A., Horwich A.L., Sigler P.B.
    Nature 371:578-586(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
  19. "Conformational variability in the refined structure of the chaperonin GroEL at 2.8-A resolution."
    Braig K., Adams P.D., Bruenger A.T.
    Nat. Struct. Biol. 2:1083-1094(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
  20. "The 2.4 A crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S."
    Boisvert D.C., Wang J., Otwinowski Z., Horwich A.L., Sigler P.B.
    Nat. Struct. Biol. 3:170-177(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
  21. "Chaperone activity and structure of monomeric polypeptide binding domains of GroEL."
    Zahn R., Buckle A.M., Perrett S., Johnson C.M., Corrales F.J., Golbik R., Fersht A.R.
    Proc. Natl. Acad. Sci. U.S.A. 93:15024-15029(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
  22. "The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex."
    Xu Z., Horwich A.L., Sigler P.B.
    Nature 388:741-750(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
  23. "The crystal structure of a GroEL/peptide complex: plasticity as a basis for substrate diversity."
    Chen L., Sigler P.B.
    Cell 99:757-768(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) OF 192-337.
  24. "Purification, crystallization and structure determination of native GroEL from Escherichia coli lacking bound potassium ions."
    Kiser P.D., Lodowski D.T., Palczewski K.
    Acta Crystallogr. F 63:457-461(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.02 ANGSTROMS).

Entry nameiCH60_ECOLI
AccessioniPrimary (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: July 9, 2014
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

This protein shows ATPase activity.

Caution

Was originally (1 Publication) designated as the ams protein.

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

External Data

Dasty 3

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