ID   CH60_GRATL              Reviewed;         528 AA.
AC   Q6B911;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 72.
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};
GN   OrderedLocusNames=Grc000043;
OS   Gracilaria tenuistipitata var. liui (Red alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gracilariales;
OC   Gracilariaceae; Agarophyton; Agarophyton tenuistipitatum.
OX   NCBI_TaxID=285951;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15638458; DOI=10.1007/s00239-004-2638-3;
RA   Hagopian J.C., Reis M., Kitajima J.P., Bhattacharya D., de Oliveira M.C.;
RT   "Comparative analysis of the complete plastid genome sequence of the red
RT   alga Gracilaria tenuistipitata var. liui provides insights into the
RT   evolution of rhodoplasts and their relationship to other plastids.";
RL   J. Mol. Evol. 59:464-477(2004).
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; AY673996; AAT79624.1; -; Genomic_DNA.
DR   RefSeq; YP_063549.1; NC_006137.1.
DR   AlphaFoldDB; Q6B911; -.
DR   SMR; Q6B911; -.
DR   GeneID; 2944044; -.
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_0000063624"
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   528 AA;  56848 MW;  F31F75390607913E CRC64;
     MAKKILYQDN ARKALEKGMD TLVEAVAITL GPKGRNVVLE RKFGAPQIIN DGVTIAKEIE
     LQDLAENTGV ALIRQAASKT NDVAGDGTTT ATVLAHAIVK QGLKNVAAGA NPITLKKGIQ
     KAVKFVVGKI AEYSKPICSM QDVTHIGSIS SGNDVEVGTM IANAIQQVGK EGIISLEEGQ
     STSTELDIKE GMKFDKGFIS PYFVTDTSRM EVIQDNPYIL ITDKKITLIQ QELLPILEKV
     TKTGRPLLII AEDIEKEALA TIIVNKLRGI INVVAVRAPG FGDRRKLLLE DIAILTSGVV
     ITQDMGLSLD SMSLDQLGSA RRVQITKDST TIVADAQKDL IQARCDQIRR QLEAATNSYA
     KDKLHERLAK LSGGVAVVKV GAATETEMRD KKLRLEDAIN ATKAAIEEGI VPGGGSTFVH
     LSEVLRVWAI NNLVEEELVG ALIIVDSLLH PLKRIVENAG NNGSIIIEKI KNSNFSTGYN
     ADIGQIVDMY KEGIIDPAKV TRSALQNAAS IASMILTTEC LIAEQVDN