ID   CH60_ENTAG              Reviewed;         539 AA.
AC   O66200; O66216;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 95.
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};
DE   Flags: Fragment;
GN   Name=groEL {ECO:0000255|HAMAP-Rule:MF_00600};
GN   Synonyms=groL {ECO:0000255|HAMAP-Rule:MF_00600}, mopA;
OS   Enterobacter agglomerans (Erwinia herbicola) (Pantoea agglomerans).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea; Pantoea agglomerans group.
OX   NCBI_TaxID=549;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 27155 / DSM 3493 / CDC 1461-67 / CIP 57.51 / JCM 1236 / KCTC
RC   2564 / LMG 1286 / NBRC 102470 / NCIMB 13953 / NCTC 9381, and
RC   JCM 7000 / CEH 803;
RX   PubMed=12501307; DOI=10.2323/jgam.43.355;
RA   Harada H., Ishikawa H.;
RT   "Phylogenetical relationship based on groE genes among phenotypically
RT   related Enterobacter, Pantoea, Klebsiella, Serratia, and Erwinia species.";
RL   J. Gen. Appl. Microbiol. 43:355-361(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; AB008142; BAA25217.1; -; Genomic_DNA.
DR   EMBL; AB008150; BAA25233.1; -; Genomic_DNA.
DR   STRING; 549.BW31_03443; -.
DR   eggNOG; COG0459; Bacteria.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0042026; P:protein refolding; IEA:InterPro.
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   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Isomerase; Nucleotide-binding.
FT   CHAIN           1..>539
FT                   /note="Chaperonin GroEL"
FT                   /id="PRO_0000063368"
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"
FT   VARIANT         98
FT                   /note="A -> S (in strain: JCM 7000)"
FT   VARIANT         122
FT                   /note="K -> Q (in strain: JCM 7000)"
FT   VARIANT         125..126
FT                   /note="AS -> IA (in strain: JCM 7000)"
FT   VARIANT         130
FT                   /note="E -> K (in strain: JCM 7000)"
FT   VARIANT         160
FT                   /note="K -> Q (in strain: JCM 7000)"
FT   VARIANT         164
FT                   /note="E -> Q (in strain: JCM 7000)"
FT   VARIANT         167
FT                   /note="D -> E (in strain: JCM 7000)"
FT   VARIANT         179
FT                   /note="D -> E (in strain: JCM 7000)"
FT   VARIANT         184
FT                   /note="E -> Q (in strain: JCM 7000)"
FT   VARIANT         213
FT                   /note="V -> I (in strain: JCM 7000)"
FT   VARIANT         248
FT                   /note="V -> L (in strain: JCM 7000)"
FT   VARIANT         294
FT                   /note="T -> I (in strain: JCM 7000)"
FT   VARIANT         313
FT                   /note="T -> A (in strain: JCM 7000)"
FT   VARIANT         341
FT                   /note="A -> T (in strain: JCM 7000)"
FT   VARIANT         347
FT                   /note="G -> T (in strain: JCM 7000)"
FT   VARIANT         351
FT                   /note="K -> Q (in strain: JCM 7000)"
FT   VARIANT         362
FT                   /note="R -> K (in strain: JCM 7000)"
FT   VARIANT         379
FT                   /note="I -> L (in strain: JCM 7000)"
FT   VARIANT         397
FT                   /note="D -> E (in strain: JCM 7000)"
FT   VARIANT         425..431
FT                   /note="KLAGLTA -> QLVDLRG (in strain: JCM 7000)"
FT   VARIANT         449
FT                   /note="A -> S (in strain: JCM 7000)"
FT   VARIANT         473
FT                   /note="E -> D (in strain: JCM 7000)"
FT   VARIANT         481
FT                   /note="A -> Q (in strain: JCM 7000)"
FT   VARIANT         524
FT                   /note="M -> L (in strain: JCM 7000)"
FT   VARIANT         534..535
FT                   /note="AA -> GGAG (in strain: JCM 7000)"
FT   NON_TER         539
SQ   SEQUENCE   539 AA;  56375 MW;  6583295F73299C3B CRC64;
     MAAKDVKFGN DARVKMLRGV NVLADAVKVT LGPKGRNVVL DKSFGAPTIT KDGVSVAREI
     ELEDKFENMG AQMVKEVASK ANDAAGDGTT TATVLAQAII TEGLKAVAAG MNPMDLKRGI
     DKAVASAVEE LKALSVPCSD SKAIAQVGTI SANSDETVGK LIAEAMDKVG KEGVITVEDG
     TGLEDELDVV EGMQFDRGYL SPYFINKPET GAVELESPFI LLADKKISNI REMLPVLEAV
     AKAGKPLVII AEDVEGEALA TLVVNTMRGI VKVAAVKAPG FGDRRKAMLQ DIATLTGGTV
     ISEEIGMELE KATLEDLGQA KRVVINKDTT TIIDGVGEEA AIQGRVGQIR KQIEEATSDY
     DREKLQERVA KLAGGVAVIK VGAATEVEMK EKKARVDDAL HATRAAVEEG VVAGGGVALV
     RVAAKLAGLT AQNEDQNVGI KVALRAMEAP LRQIVSNAGE EPSVVANNVK AGEGNYGYNA
     ATEEYGNMID FGILDPTKVT RSALQYAASV AGLMITTECM VTDMPKGDAP DLXAAGMGG