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P0A6F5

- CH60_ECOLI

UniProt

P0A6F5 - CH60_ECOLI

Protein

60 kDa chaperonin

Gene

groL

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    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.

    GO - Molecular functioni

    1. ATPase activity Source: EcoCyc
    2. ATP binding Source: EcoCyc
    3. identical protein binding Source: IntAct
    4. protein binding Source: IntAct
    5. unfolded protein binding Source: EcoCyc

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. cell cycle Source: UniProtKB-KW
    3. cell division Source: UniProtKB-KW
    4. protein folding Source: EcoCyc
    5. protein refolding Source: UniProtKB-HAMAP
    6. response to heat Source: EcoliWiki
    7. virion assembly Source: EcoliWiki

    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-RKP0A6F5.

    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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10599. groL.

    Subcellular locationi

    Cytoplasm 2 PublicationsUniRule annotation
    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.2 PublicationsCurated

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 54854760 kDa chaperoninPRO_0000063358Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    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-2DPAGEP0A6F5.

    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
    fetAP772792EBI-543750,EBI-560090
    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
    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

    1
    548
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A6F5.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the chaperonin (HSP60) family.UniRule annotation

    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]FASTAAdd to Basket

    « 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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti83 – 864DAAG → GALQ in CAA30739. (PubMed:2901493)Curated
    Sequence conflicti262 – 2621L → A in CAA30698. (PubMed:2897629)Curated
    Sequence conflicti267 – 2671M → I in CAA30698. (PubMed:2897629)Curated
    Sequence conflicti343 – 3431Q → R in AAA23934. (PubMed:2578448)Curated

    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.
    PIRiS56371. BVECGL.
    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 S56371. BVECGL.
    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...
    MobiDBi 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-2DPAGE 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-RK 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.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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 informationi

    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: October 1, 2014
    This is version 109 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 designated as the ams protein.1 Publication

    Keywords - Technical termi

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

    Documents

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

    External Data

    Dasty 3