ID   CH60_GALSU              Reviewed;         534 AA.
AC   P28256;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Chaperonin GroEL, chloroplastic {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};
OS   Galdieria sulphuraria (Red alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae; Galdieria.
OX   NCBI_TaxID=130081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=14-1-1 / Isolate 107.79/Goettingen;
RX   PubMed=1558950; DOI=10.1007/bf00020019;
RA   Kessler U., Maid U., Zetsche K.;
RT   "An equivalent to bacterial ompR genes is encoded on the plastid genome of
RT   red algae.";
RL   Plant Mol. Biol. 18:777-780(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1352188; DOI=10.1007/bf00351663;
RA   Maid U., Steinmueller R., Zetsche K.;
RT   "Structure and expression of a plastid-encoded groEL homologous heat-shock
RT   gene in a thermophilic unicellular red alga.";
RL   Curr. Genet. 21:521-525(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: Plastid, chloroplast {ECO:0000255|HAMAP-
CC       Rule:MF_00600}.
CC   -!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
CC       {ECO:0000255|HAMAP-Rule:MF_00600}.
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   EMBL; X62578; CAA44463.1; -; Genomic_DNA.
DR   AlphaFoldDB; P28256; -.
DR   SMR; P28256; -.
DR   STRING; 130081.XP_005704991.1; -.
DR   PRIDE; P28256; -.
DR   eggNOG; KOG0356; Eukaryota.
DR   GO; GO:0009507; C:chloroplast; 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; Chloroplast; Isomerase; Nucleotide-binding;
KW   Plastid.
FT   CHAIN           1..534
FT                   /note="Chaperonin GroEL, chloroplastic"
FT                   /id="PRO_0000063623"
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         414
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         496
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
SQ   SEQUENCE   534 AA;  57837 MW;  42D938B49B42114A CRC64;
     MTKQILYQEN ARKALEKGID ILAEAVSVTL GPKGRNVVIE KKYGPPQIIN DGVTIAKEIE
     LEDHIENTGV ALIRQAASKT NDVAGDGTTT STVLAHAIVK QGMRNVAAGA NPIALKRGID
     KATQFIINKI SEYSRPVEDN KAITQVATIS SGNDENIGKM IADAIEKVGR EGVISIEEGK
     STTTELEIKE GMKFERGYIS PYFVTDSDRM EVVQENASVL ITDKKITLVQ QDLLPVLEQI
     AKTNKPLLII AEDIEKEALA TLIVNKLRGI LNVVAVKAPG FGDRRKSILE DIAILTGGQL
     ITEDAGLSLD KVDLSMLGQA NKVIVNKEST TIISNANENN VKARCEQIRK QIEITDSSYE
     KEKLQERLAK LAGGIAVIKV GAATETEMKD KKLRLEDAIN ATKAAIEEGI VPGGGATLVH
     LANDLFNWAK GVLKEDELIG ALIVEKSITA PLKRIVQNEG KNGAIVVDEI KNLDFSIGYD
     ASTSKFVNMY ESGIIDPAKV TRSALQNASS IAGMILTTEC LVVDEMNRNM EVRK