ID   CH60_TRICV              Reviewed;         528 AA.
AC   P49464;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 92.
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   Trieres chinensis (Marine centric diatom) (Odontella sinensis).
OG   Plastid; Chloroplast.
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta; Mediophyceae;
OC   Biddulphiophycidae; Eupodiscales; Parodontellaceae; Trieres.
OX   NCBI_TaxID=1514140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Kowallik K.V., Stoebe B., Schaffran I., Kroth-Pancic P., Freier U.;
RT   "The chloroplast genome of a chlorophyll a+c-containing alga, Odontella
RT   sinensis.";
RL   Plant Mol. Biol. Rep. 13:336-342(1995).
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}.
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DR   EMBL; Z67753; CAA91651.1; -; Genomic_DNA.
DR   PIR; S78278; S78278.
DR   AlphaFoldDB; P49464; -.
DR   SMR; P49464; -.
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; 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; Chloroplast; Isomerase; Nucleotide-binding;
KW   Plastid.
FT   CHAIN           1..528
FT                   /note="Chaperonin GroEL, chloroplastic"
FT                   /id="PRO_0000063626"
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         415
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         481..483
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         497
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
SQ   SEQUENCE   528 AA;  57128 MW;  E04317FEC9EF2EE8 CRC64;
     MAKKILYQDN ARRALERGME IMVEAVSVTL GPKGRNVVLE KPYGSPQIVN DGVTIAKEIN
     LEDHIENTGV ALIRQAASKT NDVAGDGTTT ATVLAYAMVK EGLKNVTAGA NPISIKLGME
     KATQYLVTQI NEFAQPVEDI QSIEQVASIS AGNDNLIGSL IADALSKVGK EGVISLEEGK
     GIITELEITE GMKLEKGFIS PYFITNTEKM EVSYENPFIL LTDKRITLVQ QDLLPILEQI
     TKTKRPLLLI AEDVEKEALA TLILNKLRGI VNVVAVRAPG FGELRKQMLE DIAVLTGGTV
     ITQDAGLSLE NIQVNLLGQA RRIIVNKDST TIVGDGLEIE QIKARCEQLR KQVNIADTGY
     EKEKLQDRIA KLSGGIAVIR VGAVTETEMK DKKLRLEDAI NATRAAVEEG IVPGGGATLA
     HLAENLLTWA KINLKEDELI GAMIISRAIV APLKRIAENA GINGPVIIEK VQQQEFEIGY
     NAAKNVFGNM YDEGIVDPAK VTRSGLQNAT SIASMILTTE CIIVDETD