ID   CH60_ACIFR              Reviewed;          23 AA.
AC   P29134;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 67.
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   Acidithiobacillus ferrooxidans (Thiobacillus ferrooxidans).
OC   Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales;
OC   Acidithiobacillaceae; Acidithiobacillus.
OX   NCBI_TaxID=920;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=ATCC 19859 / BCRC 13033 / JCM 3863 / NCIMB 9490;
RX   PubMed=1360930; DOI=10.1016/0378-1097(92)90147-g;
RA   Varela P., Jerez C.A.;
RT   "Identification and characterization of GroEL and DnaK homologues in
RT   Thiobacillus ferrooxidans.";
RL   FEMS Microbiol. Lett. 77:149-153(1992).
RN   [2]
RP   PHOSPHORYLATION.
RX   PubMed=9026439; DOI=10.1111/j.1574-6968.1996.tb08145.x;
RA   Seeger M., Osorio G., Jerez C.A.;
RT   "Phosphorylation of GroEL, DnaK and other proteins from Thiobacillus
RT   ferrooxidans grown under different conditions.";
RL   FEMS Microbiol. Lett. 138:129-134(1996).
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   -!- INDUCTION: By heat shock.
CC   -!- PTM: Phosphorylated on threonine. {ECO:0000269|PubMed:9026439}.
CC   -!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
CC       {ECO:0000255|HAMAP-Rule:MF_00600, ECO:0000305}.
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DR   AlphaFoldDB; P29134; -.
DR   STRING; 380394.Lferr_0698; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Cytoplasm; Direct protein sequencing; Isomerase;
KW   Nucleotide-binding; Stress response.
FT   CHAIN           1..>23
FT                   /note="Chaperonin GroEL"
FT                   /id="PRO_0000063585"
FT   NON_TER         23
SQ   SEQUENCE   23 AA;  2536 MW;  2BB6883872FB255D CRC64;
     PAKQVAFAEH AREKMLRGVN VLA