ID   CH60_ALLVI              Reviewed;         546 AA.
AC   P31293;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Chaperonin GroEL {ECO:0000255|HAMAP-Rule:MF_00600};
DE            EC=5.6.1.7 {ECO:0000255|HAMAP-Rule:MF_00600};
DE   AltName: Full=60 kDa chaperonin {ECO:0000255|HAMAP-Rule:MF_00600};
DE   AltName: Full=Chaperonin-60 {ECO:0000255|HAMAP-Rule:MF_00600};
DE            Short=Cpn60 {ECO:0000255|HAMAP-Rule:MF_00600};
GN   Name=groEL {ECO:0000255|HAMAP-Rule:MF_00600};
GN   Synonyms=groL {ECO:0000255|HAMAP-Rule:MF_00600}, mopA;
OS   Allochromatium vinosum (Chromatium vinosum).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Allochromatium.
OX   NCBI_TaxID=1049;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8444812; DOI=10.1128/jb.175.5.1514-1523.1993;
RA   Ferreyra R., Soncini F., Viale A.M.;
RT   "Cloning, characterization, and functional expression in Escherichia coli
RT   of chaperonin (groESL) genes from the phototrophic sulfur bacterium
RT   Chromatium vinosum.";
RL   J. Bacteriol. 175:1514-1523(1993).
RN   [2]
RP   CHARACTERIZATION.
RX   PubMed=9790891; DOI=10.1006/prep.1998.0953;
RA   Dionisi H.M., Viale A.M.;
RT   "Purification and characterization of Chromatium vinosum GroEL and GroES
RT   proteins overexpressed in Escherichia coli cells lacking the endogenous
RT   groESL operon.";
RL   Protein Expr. Purif. 14:275-282(1998).
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; M99443; AAA23319.1; -; Genomic_DNA.
DR   PIR; B47073; B47073.
DR   AlphaFoldDB; P31293; -.
DR   SMR; P31293; -.
DR   PRIDE; P31293; -.
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; 1.
DR   SUPFAM; SSF52029; SSF52029; 1.
DR   SUPFAM; SSF54849; SSF54849; 1.
DR   TIGRFAMs; TIGR02348; GroEL; 1.
DR   PROSITE; PS00296; CHAPERONINS_CPN60; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Cytoplasm; Isomerase; Nucleotide-binding.
FT   CHAIN           1..546
FT                   /note="Chaperonin GroEL"
FT                   /id="PRO_0000063335"
FT   BINDING         30..33
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         51
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         87..91
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         415
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   546 AA;  57541 MW;  3250141881C04DD6 CRC64;
     MSAKDVKFGG DARVRMMEGV NILANAVKVT LGPKGRNVVL EKSFGAPTVT KDGVSVAKEI
     ELKDKFENMG AQMVKEVASK TSDIAGDGTT TATVLAQAMV REGLKAVAAG MNPMDLKRGM
     DKAVEAATEE LKKLSKPCPR PMAIAQVGTI SANSDDSIGT IIAEAMEKVG KEGVITVEDG
     TSLQNELDVV EGMQFDRGYL SPYFINNQQS QSAELDAPYI LLYDKKISNI RDLLPVLEGV
     AKAGKPLLII AEDVEGEALA TLVVNTIRGI VKVCAVKAPG FGDRRKAMLQ DIAILTGATV
     ISEEVGLSLE KATLTDLGTA KRVQVGKDET TIIDGSGSEI DIKARCEQIR AQVEETSSDY
     DREKLQERLA KLAGGVAVIK VGAATEIEMK EKKARVEDAL HATRAAVEEG IVPGGGVALV
     RAIAAVKDLK GANHDQDVGI AIARRAMEEP LRQIVANAGE EPSVILHKVA EGTGNFGYNA
     ANGEYGDMVE MGILDPTKVT RSALQNSCSV AGLMITTEAM IADEPKDDAP AMPGGGMGDM
     GGMGMM