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Q05972

- CH601_SYNY3

UniProt

Q05972 - CH601_SYNY3

Protein

60 kDa chaperonin 1

Gene

groL1

Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 4 (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.UniRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-HAMAP
    2. protein binding Source: IntAct

    GO - Biological processi

    1. protein refolding Source: UniProtKB-HAMAP
    2. response to stress Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chaperone

    Keywords - Biological processi

    Stress response

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    60 kDa chaperonin 1UniRule annotation
    Alternative name(s):
    GroEL protein 1UniRule annotation
    Protein Cpn60 1UniRule annotation
    Gene namesi
    Name:groL1UniRule annotation
    Synonyms:cpn60-1, groEL-1UniRule annotation, groEL1UniRule annotation
    Ordered Locus Names:slr2076
    OrganismiSynechocystis sp. (strain PCC 6803 / Kazusa)
    Taxonomic identifieri1111708 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis
    ProteomesiUP000001425: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 54154060 kDa chaperonin 1PRO_0000063575Add
    BLAST

    Proteomic databases

    PaxDbiQ05972.
    PRIDEiQ05972.

    Expressioni

    Inductioni

    By stress conditions e.g. heat shock.

    Interactioni

    Subunit structurei

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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    trxAP522314EBI-862119,EBI-862916

    Protein-protein interaction databases

    IntActiQ05972. 2 interactions.
    STRINGi1148.slr2076.

    Structurei

    3D structure databases

    ProteinModelPortaliQ05972.
    SMRiQ05972. Positions 2-527.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the chaperonin (HSP60) family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0459.
    HOGENOMiHOG000076290.
    KOiK04077.
    OMAiAMISANM.
    OrthoDBiEOG6JDWBZ.
    PhylomeDBiQ05972.

    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.

    Q05972-1 [UniParc]FASTAAdd to Basket

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    MAKSIIYNDE ARRALERGMD ILAEAVAVTL GPKGRNVVLE KKFGSPQIIN    50
    DGITIAKEIE LEDHVENTGV SLIRQAASKT NDVAGDGTTT ATVLAHAIVK 100
    EGLRNVAAGA NPISLKRGID KATDFLVARI KEHAQPVGDS KAIAQVGAIS 150
    AGNDEEVGQM IANAMDKVGQ EGVISLEEGK SMTTELEITE GMRFDKGYIS 200
    PYFVTDAERM EAVLEDPRIL ITDKKINLVQ DLVPILEQVA RQGKPLLIIA 250
    EDIEKEALAT LVVNRLRGVL NVAAVKAPGF GDRRKQMLED IATLTGGQVI 300
    SEDAGLKLES ATVDSLGSAR RINITKDNTT IVAEGNEAAV KSRCEQIRRQ 350
    IEETDSSYDK EKLQERLAKL AGGVAVIKVG AATETEMKDR KLRLEDAINA 400
    TKAAVEEGIV PGGGTTLAHL APQLEDWATG NLKDEELTGA LIVARALPAP 450
    LKRIAENAGQ NGAVISERVK EKEFNVGYNA ASLEYVDMLA AGIVDPAKVT 500
    RSALQNAASI AGMVLTTECI VVDKPEKEKA PAGAPGGDFD Y 541
    Length:541
    Mass (Da):57,653
    Last modified:January 23, 2007 - v4
    Checksum:i37E158A939CBFCB8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti12 – 121R → T AA sequence (PubMed:1346251)Curated
    Sequence conflicti91 – 911A → D in BAA02180. (PubMed:8093614)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D12677 Genomic DNA. Translation: BAA02180.1.
    BA000022 Genomic DNA. Translation: BAA17411.1.
    PIRiB44425.
    RefSeqiNP_440731.1. NC_000911.1.
    YP_005650790.1. NC_017277.1.
    YP_007450614.1. NC_020286.1.

    Genome annotation databases

    EnsemblBacteriaiBAA17411; BAA17411; BAA17411.
    GeneIDi954034.
    KEGGisyn:slr2076.
    syy:SYNGTS_0837.
    syz:MYO_18420.
    PATRICi23838680. VBISynSp132158_0907.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D12677 Genomic DNA. Translation: BAA02180.1 .
    BA000022 Genomic DNA. Translation: BAA17411.1 .
    PIRi B44425.
    RefSeqi NP_440731.1. NC_000911.1.
    YP_005650790.1. NC_017277.1.
    YP_007450614.1. NC_020286.1.

    3D structure databases

    ProteinModelPortali Q05972.
    SMRi Q05972. Positions 2-527.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q05972. 2 interactions.
    STRINGi 1148.slr2076.

    Proteomic databases

    PaxDbi Q05972.
    PRIDEi Q05972.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAA17411 ; BAA17411 ; BAA17411 .
    GeneIDi 954034.
    KEGGi syn:slr2076.
    syy:SYNGTS_0837.
    syz:MYO_18420.
    PATRICi 23838680. VBISynSp132158_0907.

    Phylogenomic databases

    eggNOGi COG0459.
    HOGENOMi HOG000076290.
    KOi K04077.
    OMAi AMISANM.
    OrthoDBi EOG6JDWBZ.
    PhylomeDBi Q05972.

    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. "A second groEL-like gene, organized in a groESL operon is present in the genome of Synechocystis sp. PCC 6803."
      Lehel C., Los D.A., Wada H., Gyorgyei J., Horvath I., Kovacs E., Murata N., Vigh L.
      J. Biol. Chem. 268:1799-1804(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-26.
    2. "Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions."
      Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.
      , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
      DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: PCC 6803 / Kazusa.
    3. "Towards a proteome project of cyanobacterium Synechocystis sp. strain PCC6803: linking 130 protein spots with their respective genes."
      Sazuka T., Ohara O.
      Electrophoresis 18:1252-1258(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-21.
    4. "Heat shock protein synthesis of the cyanobacterium Synechocystis PCC 6803: purification of the GroEL-related chaperonin."
      Lehel C., Wada H., Kovacs E., Toroek Z., Gombos Z., Horvath I., Murata N., Vigh L.
      Plant Mol. Biol. 18:327-336(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-26.

    Entry informationi

    Entry nameiCH601_SYNY3
    AccessioniPrimary (citable) accession number: Q05972
    Secondary accession number(s): P73379
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 108 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Synechocystis PCC 6803
      Synechocystis (strain PCC 6803): entries and gene names

    External Data

    Dasty 3