ID   CH60_STRAP              Reviewed;         540 AA.
AC   Q8KJ20;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 87.
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};
GN   Name=groEL {ECO:0000255|HAMAP-Rule:MF_00600};
GN   Synonyms=groL {ECO:0000255|HAMAP-Rule:MF_00600};
OS   Streptococcus anginosus.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus; Streptococcus anginosus group.
OX   NCBI_TaxID=1328;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12202549; DOI=10.1128/jcm.40.9.3172-3178.2002;
RA   Teng L.-J., Hsueh P.R., Tsai J.C., Chen P.-W., Hsu J.-C., Lai H.C.,
RA   Lee C.N., Ho S.W.;
RT   "groESL sequence determination, phylogenetic analysis, and species
RT   differentiation for viridans group streptococci.";
RL   J. Clin. Microbiol. 40:3172-3178(2002).
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}.
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; AF378195; AAM46144.1; -; Genomic_DNA.
DR   RefSeq; WP_003026907.1; NZ_LR134283.1.
DR   AlphaFoldDB; Q8KJ20; -.
DR   SMR; Q8KJ20; -.
DR   STRING; 862971.SANR_0269; -.
DR   GeneID; 58054723; -.
DR   eggNOG; COG0459; Bacteria.
DR   OrthoDB; 265347at2; -.
DR   GO; GO:0005737; C:cytoplasm; 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; Cytoplasm; Isomerase; Nucleotide-binding.
FT   CHAIN           1..540
FT                   /note="Chaperonin GroEL"
FT                   /id="PRO_0000063546"
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         413
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         476..478
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT   BINDING         492
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
SQ   SEQUENCE   540 AA;  56904 MW;  A1A02E7F09EE6634 CRC64;
     MAKDIKFSAD ARSAMVRGVD ILADTVKVTL GPKGRNVVLE KSFGSPLITN DGVTIAKEIE
     LEDHFENMGA KLVSEVASKT NDIAGDGTTT ATVLTQAIVR EGIKNVTAGA NPIGIRRGIE
     TAVATAVEAL KANSVPVSNK EAIAQVAAVS SRSEKVGEYI SEAMEKVGND GVITIEESKG
     METELDVVEG MQFDRGYLSQ YMVTDNEKMV ADLDNPYILI TDKKISNIQE ILPLLENILK
     TSRPLLIIAD DVDGEALPTL VLNKIRGTFN VVAVKAPGFG DRRKAMLEDI AILTGGTVIT
     EDLGLELKDA TIEALGQASK VTVDKDSTVI VEGSGDAEAI ANRVAVIKSQ IESSTSDFDR
     EKLQERLAKL SGGVAVIKVG AATETELKEM KLRIEDALNA TRAAVEEGIV SGGGTAFVNV
     LSAVEALDLS GDEATGRNIV LRALEEPVRQ IALNAGFEGS IVIDRLKNSE AGTGFNAATG
     EWVNMIDAGI IDPVKVTRSA LQNAASVASL ILTTEAVVAN QPEPASPTPA MDPSMMGGMM