ID   CH60_PYRSA              Reviewed;         585 AA.
AC   P46224;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, 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=cpn60, groL {ECO:0000255|HAMAP-Rule:MF_00600};
OS   Pyrenomonas salina.
OG   Plastid; Chloroplast.
OC   Eukaryota; Cryptophyceae; Pyrenomonadales; Pyrenomonadaceae; Pyrenomonas.
OX   NCBI_TaxID=3034;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7823908; DOI=10.1007/bf00290141;
RA   Maier U.-G., Rensing S.A., Igloi G.L., Maerz M.;
RT   "Twintrons are not unique to the Euglena chloroplast genome: structure and
RT   evolution of a plastome cpn60 gene from a cryptomonad.";
RL   Mol. Gen. Genet. 246:128-131(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; X81356; CAA57124.1; -; Genomic_DNA.
DR   PIR; S49253; S49253.
DR   AlphaFoldDB; P46224; -.
DR   SMR; P46224; -.
DR   PRIDE; P46224; -.
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:0016730; F:oxidoreductase activity, acting on iron-sulfur proteins as donors; IEA:InterPro.
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; IPR036644; FTR_bsu_sf.
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   SUPFAM; SSF57662; SSF57662; 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..585
FT                   /note="Chaperonin GroEL, chloroplastic"
FT                   /id="PRO_0000063628"
FT   BINDING         55..58
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         113..117
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         442
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         507..509
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         523
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
SQ   SEQUENCE   585 AA;  64243 MW;  BC54A5835ED36682 CRC64;
     MRRFSETYGQ KKQITFFCSN LSITAVVIEG LLKHKEEYGA LERGMDILAE AVSVTLGPKG
     RNVVLESGKY GPPQIVNDGV TIAKEIELED HIENTGVALI RQAASKTNDV AGDGTTTATV
     LAHAMVKQGM KNVRCRSKSI AIKRGIEKAT QFVISQIAEY SRPVEDTKSI TQVAAISAGN
     DMEVGQMIAD AIEKVGREGV ISLEEGKSTV TELELTEGNG WFLKKGFISP YFVTDTDRME
     TTQENPYILL TDKKISLVQE LVPIHLELIS KTSRPLLIIA EDVEKEALAT LVVNKLRGIV
     NVVAVRAPGF GDRRKTMLED IAILTGGQVI SEDAGFSLET VQLDMLGQAR RITVVKEGTT
     IIAEGHEREV KARCEQIRRQ IEASESSYER EKLQERLAKL AGGVAVIKVG AATETEKDKK
     LRLEDAINAT KAAVEEGIVP GGATLIHFIE DLNDWAEDNL LDDELIGALI VEKALSAPMK
     RIIENTGISS SIIIEKIKDK DFSIGYNAAQ GEIEDMYEIG VIDPAKVTRS AMQNAASIAS
     MILTTECIVV DKKKTCSLET SIYWLVLTNK YFCLDLLRLY FFLKD