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P0A6F9

- CH10_ECOLI

UniProt

P0A6F9 - CH10_ECOLI

Protein

10 kDa chaperonin

Gene

groS

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.

    GO - Molecular functioni

    1. ATP binding Source: InterPro
    2. identical protein binding Source: IntAct
    3. protein binding Source: IntAct
    4. unfolded protein binding Source: EcoCyc

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. cell division Source: UniProtKB-KW
    3. protein folding Source: UniProtKB-HAMAP
    4. response to heat Source: EcoliWiki
    5. virion assembly Source: EcoliWiki

    Keywords - Molecular functioni

    Chaperone

    Keywords - Biological processi

    Cell cycle, Cell division

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10600-MONOMER.
    ECOL316407:JW4102-MONOMER.
    SABIO-RKP0A6F9.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    10 kDa chaperonin
    Alternative name(s):
    GroES protein
    Protein Cpn10
    Gene namesi
    Name:groS
    Synonyms:groES, mopB
    Ordered Locus Names:b4142, JW4102
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10600. groS.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cytosol Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 979710 kDa chaperoninPRO_0000174746Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei34 – 341N6-succinyllysine1 Publication

    Proteomic databases

    PaxDbiP0A6F9.
    PRIDEiP0A6F9.

    2D gel databases

    SWISS-2DPAGEP0A6F9.

    PTM databases

    PhosSiteiP0809397.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A6F9.

    Interactioni

    Subunit structurei

    Heptamer of 7 subunits arranged in a ring.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-369169,EBI-369169
    groLP0A6F525EBI-369169,EBI-543750

    Protein-protein interaction databases

    DIPiDIP-9835N.
    IntActiP0A6F9. 28 interactions.
    MINTiMINT-5232475.
    STRINGi511145.b4142.

    Structurei

    Secondary structure

    1
    97
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 54
    Beta strandi7 – 148
    Turni20 – 234
    Beta strandi37 – 437
    Beta strandi45 – 473
    Beta strandi51 – 533
    Beta strandi64 – 674
    Beta strandi74 – 785
    Beta strandi81 – 877
    Helixi88 – 903
    Beta strandi91 – 966

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AONX-ray3.00O/P/Q/R/S/T/U1-97[»]
    1EGSNMR-A19-27[»]
    1GRUelectron microscopy12.50O/P/Q/R/S/T/U1-97[»]
    1PCQX-ray2.81O/P/Q/R/S/T/U1-97[»]
    1PF9X-ray2.99O/P/Q/R/S/T/U1-97[»]
    1SVTX-ray2.81O/P/Q/R/S/T/U1-97[»]
    1SX4X-ray3.00O/P/Q/R/S/T/U1-97[»]
    2C7Celectron microscopy7.70O/P/Q/R/S/T/U1-97[»]
    2C7Delectron microscopy8.70O/P/Q/R/S/T/U1-97[»]
    3ZPZelectron microscopy8.90O/P/Q/R/S/T/U1-97[»]
    3ZQ0electron microscopy9.20O/P/Q/R/S/T/U1-97[»]
    3ZQ1electron microscopy15.90O/P/Q/R/S/T/U1-97[»]
    ProteinModelPortaliP0A6F9.
    SMRiP0A6F9. Positions 1-97.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A6F9.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the GroES chaperonin family.Curated

    Phylogenomic databases

    eggNOGiCOG0234.
    HOGENOMiHOG000133897.
    KOiK04078.
    OMAiGYGVKVE.
    OrthoDBiEOG6GFGSD.
    PhylomeDBiP0A6F9.

    Family and domain databases

    Gene3Di2.30.33.40. 1 hit.
    HAMAPiMF_00580. CH10.
    InterProiIPR020818. Chaperonin_Cpn10.
    IPR018369. Chaprnonin_Cpn10_CS.
    IPR011032. GroES-like.
    [Graphical view]
    PANTHERiPTHR10772. PTHR10772. 1 hit.
    PfamiPF00166. Cpn10. 1 hit.
    [Graphical view]
    PRINTSiPR00297. CHAPERONIN10.
    SMARTiSM00883. Cpn10. 1 hit.
    [Graphical view]
    SUPFAMiSSF50129. SSF50129. 1 hit.
    PROSITEiPS00681. CHAPERONINS_CPN10. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0A6F9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNIRPLHDRV IVKRKEVETK SAGGIVLTGS AAAKSTRGEV LAVGNGRILE   50
    NGEVKPLDVK VGDIVIFNDG YGVKSEKIDN EEVLIMSESD ILAIVEA 97
    Length:97
    Mass (Da):10,387
    Last modified:March 29, 2005 - v1
    Checksum:i76829E09B11217EF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti89 – 891S → N in CAA30738. (PubMed:2901493)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X07850 Genomic DNA. Translation: CAA30697.1.
    X07899 Genomic DNA. Translation: CAA30738.1.
    U14003 Genomic DNA. Translation: AAA97041.1.
    U00096 Genomic DNA. Translation: AAC77102.1.
    AP009048 Genomic DNA. Translation: BAE78144.1.
    PIRiS03931. BVECGS.
    RefSeqiNP_418566.1. NC_000913.3.
    YP_492285.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC77102; AAC77102; b4142.
    BAE78144; BAE78144; BAE78144.
    GeneIDi12933204.
    948655.
    KEGGiecj:Y75_p4029.
    eco:b4142.
    PATRICi32123853. VBIEscCol129921_4274.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X07850 Genomic DNA. Translation: CAA30697.1 .
    X07899 Genomic DNA. Translation: CAA30738.1 .
    U14003 Genomic DNA. Translation: AAA97041.1 .
    U00096 Genomic DNA. Translation: AAC77102.1 .
    AP009048 Genomic DNA. Translation: BAE78144.1 .
    PIRi S03931. BVECGS.
    RefSeqi NP_418566.1. NC_000913.3.
    YP_492285.1. 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 O/P/Q/R/S/T/U 1-97 [» ]
    1EGS NMR - A 19-27 [» ]
    1GRU electron microscopy 12.50 O/P/Q/R/S/T/U 1-97 [» ]
    1PCQ X-ray 2.81 O/P/Q/R/S/T/U 1-97 [» ]
    1PF9 X-ray 2.99 O/P/Q/R/S/T/U 1-97 [» ]
    1SVT X-ray 2.81 O/P/Q/R/S/T/U 1-97 [» ]
    1SX4 X-ray 3.00 O/P/Q/R/S/T/U 1-97 [» ]
    2C7C electron microscopy 7.70 O/P/Q/R/S/T/U 1-97 [» ]
    2C7D electron microscopy 8.70 O/P/Q/R/S/T/U 1-97 [» ]
    3ZPZ electron microscopy 8.90 O/P/Q/R/S/T/U 1-97 [» ]
    3ZQ0 electron microscopy 9.20 O/P/Q/R/S/T/U 1-97 [» ]
    3ZQ1 electron microscopy 15.90 O/P/Q/R/S/T/U 1-97 [» ]
    ProteinModelPortali P0A6F9.
    SMRi P0A6F9. Positions 1-97.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-9835N.
    IntActi P0A6F9. 28 interactions.
    MINTi MINT-5232475.
    STRINGi 511145.b4142.

    PTM databases

    PhosSitei P0809397.

    2D gel databases

    SWISS-2DPAGE P0A6F9.

    Proteomic databases

    PaxDbi P0A6F9.
    PRIDEi P0A6F9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC77102 ; AAC77102 ; b4142 .
    BAE78144 ; BAE78144 ; BAE78144 .
    GeneIDi 12933204.
    948655.
    KEGGi ecj:Y75_p4029.
    eco:b4142.
    PATRICi 32123853. VBIEscCol129921_4274.

    Organism-specific databases

    EchoBASEi EB0595.
    EcoGenei EG10600. groS.

    Phylogenomic databases

    eggNOGi COG0234.
    HOGENOMi HOG000133897.
    KOi K04078.
    OMAi GYGVKVE.
    OrthoDBi EOG6GFGSD.
    PhylomeDBi P0A6F9.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10600-MONOMER.
    ECOL316407:JW4102-MONOMER.
    SABIO-RK P0A6F9.

    Miscellaneous databases

    EvolutionaryTracei P0A6F9.
    PROi P0A6F9.

    Gene expression databases

    Genevestigatori P0A6F9.

    Family and domain databases

    Gene3Di 2.30.33.40. 1 hit.
    HAMAPi MF_00580. CH10.
    InterProi IPR020818. Chaperonin_Cpn10.
    IPR018369. Chaprnonin_Cpn10_CS.
    IPR011032. GroES-like.
    [Graphical view ]
    PANTHERi PTHR10772. PTHR10772. 1 hit.
    Pfami PF00166. Cpn10. 1 hit.
    [Graphical view ]
    PRINTSi PR00297. CHAPERONIN10.
    SMARTi SM00883. Cpn10. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50129. SSF50129. 1 hit.
    PROSITEi PS00681. CHAPERONINS_CPN10. 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. "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].
    3. "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.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    5. "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.
    6. "Identification of nucleotide-binding regions in the chaperonin proteins GroEL and GroES."
      Martin J., Geromanos S., Tempst P., Hartl F.U.
      Nature 366:279-282(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 61-74.
    7. "Identifying proteins from two-dimensional gels by molecular mass searching of peptide fragments in protein sequence databases."
      Henzel W.J., Billeci T.M., Stults J.T., Wong S.C., Grimley C., Watanabe C.
      Proc. Natl. Acad. Sci. U.S.A. 90:5011-5015(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-18.
    8. Cited for: PROTEIN SEQUENCE OF 1-11.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    9. "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 1-12.
      Strain: K12 / EMG2.
    10. Cited for: PROTEIN SEQUENCE OF 1-4.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    11. "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.
    12. "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.
      Strain: K12.
    13. "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.
    14. "The crystal structure of the GroES co-chaperonin at 2.8-A resolution."
      Hunt J.F., Weaver A.J., Landry S.J., Gierasch L., Deisenhofer J.
      Nature 379:37-45(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
    15. "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).
    16. Cited for: STRUCTURE BY NMR OF 19-27.

    Entry informationi

    Entry nameiCH10_ECOLI
    AccessioniPrimary (citable) accession number: P0A6F9
    Secondary accession number(s): P05380, Q2M6G2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2005
    Last sequence update: March 29, 2005
    Last modified: October 1, 2014
    This is version 98 of the entry and version 1 of the sequence. [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. 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