ID   CH601_SYNY3             Reviewed;         541 AA.
AC   Q05972; P73379;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   27-MAR-2024, entry version 157.
DE   RecName: Full=Chaperonin GroEL 1 {ECO:0000255|HAMAP-Rule:MF_00600};
DE            EC=5.6.1.7 {ECO:0000255|HAMAP-Rule:MF_00600};
DE   AltName: Full=60 kDa chaperonin 1 {ECO:0000255|HAMAP-Rule:MF_00600};
DE   AltName: Full=Chaperonin-60 1 {ECO:0000255|HAMAP-Rule:MF_00600};
DE            Short=Cpn60 1 {ECO:0000255|HAMAP-Rule:MF_00600};
GN   Name=groEL1 {ECO:0000255|HAMAP-Rule:MF_00600};
GN   Synonyms=cpn60-1, groL1 {ECO:0000255|HAMAP-Rule:MF_00600};
GN   OrderedLocusNames=slr2076;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae;
OC   Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-26.
RX   PubMed=8093614; DOI=10.1016/s0021-9258(18)53924-7;
RA   Lehel C., Los D.A., Wada H., Gyorgyei J., Horvath I., Kovacs E., Murata N.,
RA   Vigh L.;
RT   "A second groEL-like gene, organized in a groESL operon is present in the
RT   genome of Synechocystis sp. PCC 6803.";
RL   J. Biol. Chem. 268:1799-1804(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-21.
RX   PubMed=9298645; DOI=10.1002/elps.1150180806;
RA   Sazuka T., Ohara O.;
RT   "Towards a proteome project of cyanobacterium Synechocystis sp. strain
RT   PCC6803: linking 130 protein spots with their respective genes.";
RL   Electrophoresis 18:1252-1258(1997).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-26.
RX   PubMed=1346251; DOI=10.1007/bf00034959;
RA   Lehel C., Wada H., Kovacs E., Toroek Z., Gombos Z., Horvath I., Murata N.,
RA   Vigh L.;
RT   "Heat shock protein synthesis of the cyanobacterium Synechocystis PCC 6803:
RT   purification of the GroEL-related chaperonin.";
RL   Plant Mol. Biol. 18:327-336(1992).
CC   -!- FUNCTION: Together with its co-chaperonin GroES, plays an essential
CC       role in assisting protein folding. The GroEL-GroES system forms a nano-
CC       cage that allows encapsulation of the non-native substrate proteins and
CC       provides a physical environment optimized to promote and accelerate
CC       protein folding. {ECO:0000255|HAMAP-Rule:MF_00600}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + a folded polypeptide = ADP + phosphate + an
CC         unfolded polypeptide.; EC=5.6.1.7; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00600};
CC   -!- SUBUNIT: Forms a cylinder of 14 subunits composed of two heptameric
CC       rings stacked back-to-back. Interacts with the co-chaperonin GroES.
CC       {ECO:0000255|HAMAP-Rule:MF_00600}.
CC   -!- INTERACTION:
CC       Q05972; P52231: trxA; NbExp=4; IntAct=EBI-862119, EBI-862916;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00600}.
CC   -!- INDUCTION: By stress conditions e.g. heat shock.
CC   -!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
CC       {ECO:0000255|HAMAP-Rule:MF_00600}.
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DR   EMBL; D12677; BAA02180.1; -; Genomic_DNA.
DR   EMBL; BA000022; BAA17411.1; -; Genomic_DNA.
DR   PIR; B44425; B44425.
DR   AlphaFoldDB; Q05972; -.
DR   SMR; Q05972; -.
DR   IntAct; Q05972; 2.
DR   STRING; 1148.gene:10498274; -.
DR   PaxDb; 1148-1652489; -.
DR   EnsemblBacteria; BAA17411; BAA17411; BAA17411.
DR   KEGG; syn:slr2076; -.
DR   eggNOG; COG0459; Bacteria.
DR   InParanoid; Q05972; -.
DR   PhylomeDB; Q05972; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:1990220; C:GroEL-GroES complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR   GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR   GO; GO:0009408; P:response to heat; IBA:GO_Central.
DR   CDD; cd03344; GroEL; 1.
DR   Gene3D; 3.50.7.10; GroEL; 1.
DR   Gene3D; 1.10.560.10; GroEL-like equatorial domain; 1.
DR   Gene3D; 3.30.260.10; TCP-1-like chaperonin intermediate domain; 1.
DR   HAMAP; MF_00600; CH60; 1.
DR   InterPro; IPR018370; Chaperonin_Cpn60_CS.
DR   InterPro; IPR001844; Cpn60/GroEL.
DR   InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR   InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR   InterPro; IPR027413; GROEL-like_equatorial_sf.
DR   InterPro; IPR027410; TCP-1-like_intermed_sf.
DR   NCBIfam; TIGR02348; GroEL; 1.
DR   PANTHER; PTHR45633; 60 KDA HEAT SHOCK PROTEIN, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR45633:SF3; 60 KDA HEAT SHOCK PROTEIN, MITOCHONDRIAL; 1.
DR   Pfam; PF00118; Cpn60_TCP1; 1.
DR   PRINTS; PR00298; CHAPERONIN60.
DR   SUPFAM; SSF52029; GroEL apical domain-like; 1.
DR   SUPFAM; SSF48592; GroEL equatorial domain-like; 1.
DR   SUPFAM; SSF54849; GroEL-intermediate domain like; 1.
DR   PROSITE; PS00296; CHAPERONINS_CPN60; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Cytoplasm; Direct protein sequencing; Isomerase;
KW   Nucleotide-binding; Reference proteome; Stress response.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1346251,
FT                   ECO:0000269|PubMed:8093614, ECO:0000269|PubMed:9298645"
FT   CHAIN           2..541
FT                   /note="Chaperonin GroEL 1"
FT                   /id="PRO_0000063575"
FT   BINDING         29..32
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         86..90
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         413
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         479..481
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         495
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   CONFLICT        12
FT                   /note="R -> T (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        91
FT                   /note="A -> D (in Ref. 1; BAA02180)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   541 AA;  57653 MW;  37E158A939CBFCB8 CRC64;
     MAKSIIYNDE ARRALERGMD ILAEAVAVTL GPKGRNVVLE KKFGSPQIIN DGITIAKEIE
     LEDHVENTGV SLIRQAASKT NDVAGDGTTT ATVLAHAIVK EGLRNVAAGA NPISLKRGID
     KATDFLVARI KEHAQPVGDS KAIAQVGAIS AGNDEEVGQM IANAMDKVGQ EGVISLEEGK
     SMTTELEITE GMRFDKGYIS PYFVTDAERM EAVLEDPRIL ITDKKINLVQ DLVPILEQVA
     RQGKPLLIIA EDIEKEALAT LVVNRLRGVL NVAAVKAPGF GDRRKQMLED IATLTGGQVI
     SEDAGLKLES ATVDSLGSAR RINITKDNTT IVAEGNEAAV KSRCEQIRRQ IEETDSSYDK
     EKLQERLAKL AGGVAVIKVG AATETEMKDR KLRLEDAINA TKAAVEEGIV PGGGTTLAHL
     APQLEDWATG NLKDEELTGA LIVARALPAP LKRIAENAGQ NGAVISERVK EKEFNVGYNA
     ASLEYVDMLA AGIVDPAKVT RSALQNAASI AGMVLTTECI VVDKPEKEKA PAGAPGGDFD
     Y
//