ID   CH60_DELAC              Reviewed;          25 AA.
AC   Q9R5K5;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 2.
DT   03-AUG-2022, entry version 49.
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};
OS   Delftia acidovorans (Pseudomonas acidovorans) (Comamonas acidovorans).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Delftia.
OX   NCBI_TaxID=80866;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=MC1;
RX   PubMed=15073309; DOI=10.1099/mic.0.26774-0;
RA   Benndorf D., Davidson I., Babel W.;
RT   "Regulation of catabolic enzymes during long-term exposure of Delftia
RT   acidovorans MC1 to chlorophenoxy herbicides.";
RL   Microbiology 150:1005-1014(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-15.
RC   STRAIN=PHB13.21;
RX   PubMed=1352616; DOI=10.1111/j.1365-2958.1992.tb00880.x;
RA   Fowell S.L., Lilley K.S., Jones D., Maxwell A.;
RT   "GroEL proteins from three Pseudomonas species.";
RL   Mol. Microbiol. 6:1575-1576(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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00600}.
CC   -!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
CC       {ECO:0000255|HAMAP-Rule:MF_00600, ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   PIR; S11805; S11805.
DR   AlphaFoldDB; Q9R5K5; -.
DR   SMR; Q9R5K5; -.
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.
FT   CHAIN           1..>25
FT                   /note="Chaperonin GroEL"
FT                   /id="PRO_0000063346"
FT   CONFLICT        1
FT                   /note="H -> A (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   NON_TER         25
SQ   SEQUENCE   25 AA;  2625 MW;  194DAA9115F77345 CRC64;
     HAKDVVFGGE ARARMVEGVN ILANA