ID   CH601_THEVL             Reviewed;         545 AA.
AC   O50323;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 96.
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=groL1 {ECO:0000255|HAMAP-Rule:MF_00600};
OS   Thermostichus vulcanus (Synechococcus vulcanus).
OC   Bacteria; Cyanobacteria; Thermostichales; Thermostichaceae; Thermostichus.
OX   NCBI_TaxID=32053;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9434123; DOI=10.1016/s0167-4838(97)00159-3;
RA   Tanaka N., Hiyama T., Nakamoto H.;
RT   "Cloning, characterization and functional analysis of groESL operon from
RT   thermophilic cyanobacterium Synechococcus vulcanus.";
RL   Biochim. Biophys. Acta 1343:335-348(1997).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00600}.
CC   -!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
CC       {ECO:0000255|HAMAP-Rule:MF_00600}.
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DR   EMBL; D78139; BAA23817.1; -; Genomic_DNA.
DR   AlphaFoldDB; O50323; -.
DR   SMR; O50323; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; IEA:UniProtKB-UniRule.
DR   GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR   CDD; cd03344; GroEL; 1.
DR   Gene3D; 1.10.560.10; -; 1.
DR   Gene3D; 3.30.260.10; -; 1.
DR   Gene3D; 3.50.7.10; -; 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   Pfam; PF00118; Cpn60_TCP1; 1.
DR   PRINTS; PR00298; CHAPERONIN60.
DR   SUPFAM; SSF48592; SSF48592; 2.
DR   SUPFAM; SSF52029; SSF52029; 1.
DR   TIGRFAMs; TIGR02348; GroEL; 1.
DR   PROSITE; PS00296; CHAPERONINS_CPN60; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Isomerase; Nucleotide-binding.
FT   CHAIN           1..545
FT                   /note="Chaperonin GroEL 1"
FT                   /id="PRO_0000063572"
FT   REGION          525..545
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
SQ   SEQUENCE   545 AA;  58268 MW;  9E5BC40977F75D30 CRC64;
     MAKRIIYNEN ARRALEKGMD ILAESVAVTL GPKGRNVVLE KKFGAPQIVN DGVTIAKEIE
     LEDHIENTGV ALIRQAASKT NDAAGDGTTT ATVLAHAMVK EGLRNVAAGA NPIALKRGID
     KATQFLVEKI AEHARPVEDS KAIAQVAAIS AGNDEEVGRM IADAMDKVGK EGVISLEEAK
     SMTTELEVTE GMRFDKGYIS PYFATDTERM EAVLDEPFVL VTDKKITLVQ DLVPILEQVA
     RAGKPLVIIA EDIEKEALAT LVVNRLRGVL NVAAVKAPGF GDRSKAMLED IAVLTAGQVI
     AEDAGLKLEN AKLDMLGKAR RITITKDHTT IVAEGNEKAV KARCEQIRRQ IEETDSSYDK
     EKLQERLAKL AGGVAVIKVG AATETEMKDR KLRLEDAINA TKAAVEEGIV PGGGTTLVHL
     APELSNWAAE HLTGEELIGA NIVERALSAP LRRIAENAGQ NGAIIVERVK EKPFDVGYDA
     AKDEYVNMFD AGIVDPAKVT RSALQNAASI AGMVLTTECI IVDKPEPKEN NPAGSGAGMG
     GDFDY