CH60_THET8
ID CH60_THET8 Reviewed; 543 AA.
AC Q5SLM2;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 106.
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};
DE AltName: Full=Heat shock protein 60;
GN Name=groEL {ECO:0000255|HAMAP-Rule:MF_00600};
GN Synonyms=cpnL, groL {ECO:0000255|HAMAP-Rule:MF_00600}, hsp60, mopA;
GN OrderedLocusNames=TTHA0271;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=8543569; DOI=10.1093/oxfordjournals.jbchem.a124913;
RA Amada K., Yohda M., Odaka M., Endo I., Ishii N., Taguchi H., Yoshida M.;
RT "Molecular cloning, expression, and characterization of chaperonin-60 and
RT chaperonin-10 from a thermophilic bacterium, Thermus thermophilus HB8.";
RL J. Biochem. 118:347-354(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Erbeznik M., Joachimiak A.;
RT "Cloning and characterization of the GroESL operon in Thermus aquaticus
RT HB8.";
RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 2-44.
RX PubMed=1682319; DOI=10.1016/s0021-9258(18)54588-9;
RA Taguchi H., Konishi J., Ishii N., Yoshida M.;
RT "A chaperonin from a thermophilic bacterium, Thermus thermophilus, that
RT controls refoldings of several thermophilic enzymes.";
RL J. Biol. Chem. 266:22411-22418(1991).
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 -!- INTERACTION:
CC Q5SLM2; P61493: groES; NbExp=2; IntAct=EBI-15757498, EBI-15757522;
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}.
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DR EMBL; D45880; BAA08299.1; -; Genomic_DNA.
DR EMBL; U29483; AAA83441.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD70094.1; -; Genomic_DNA.
DR PIR; A39313; A39313.
DR RefSeq; WP_011174077.1; NC_006461.1.
DR RefSeq; YP_143537.1; NC_006461.1.
DR AlphaFoldDB; Q5SLM2; -.
DR SMR; Q5SLM2; -.
DR DIP; DIP-48331N; -.
DR IntAct; Q5SLM2; 1.
DR STRING; 300852.55771653; -.
DR EnsemblBacteria; BAD70094; BAD70094; BAD70094.
DR GeneID; 3168209; -.
DR KEGG; ttj:TTHA0271; -.
DR PATRIC; fig|300852.9.peg.271; -.
DR eggNOG; COG0459; Bacteria.
DR HOGENOM; CLU_016503_3_0_0; -.
DR OMA; TDTDKME; -.
DR PhylomeDB; Q5SLM2; -.
DR Proteomes; UP000000532; Chromosome.
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 1: Evidence at protein level;
KW ATP-binding; Chaperone; Cytoplasm; Direct protein sequencing; Isomerase;
KW Nucleotide-binding; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1682319"
FT CHAIN 2..543
FT /note="Chaperonin GroEL"
FT /id="PRO_0000063582"
FT REGION 524..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 29..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 50
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 480..482
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"
FT CONFLICT 35
FT /note="R -> N (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="A -> R (in Ref. 2; AAA83441)"
FT /evidence="ECO:0000305"
FT CONFLICT 437..440
FT /note="TGAK -> RAPE (in Ref. 2; AAA83441)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 543 AA; 57889 MW; 2F4E42EA89F3C3D3 CRC64;
MAKILVFDEA ARRALERGVN AVANAVKVTL GPRGRNVVLE KKFGSPTITK DGVTVAKEVE
LEDHLENIGA QLLKEVASKT NDVAGDGTTT ATVLAQAIVR EGLKNVAAGA NPLALKRGIE
KAVEAAVEKI KALAIPVEDR KAIEEVATIS ANDPEVGKLI ADAMEKVGKE GIITVEESKS
LETELKFVEG YQFDKGYISP YFVTNPETME AVLEDAFILI VEKKVSNVRE LLPILEQVAQ
TGKPLLIIAE DVEGEALATL VVNKLRGTLS VAAVKAPGFG DRRKEMLKDI AAVTGGTVIS
EELGFKLENA TLSMLGRAER VRITKDETTI VGGKGKKEDI EARINGIKKE LETTDSEYAR
EKLQERLAKL AGGVAVIRVG AATETELKEK KHRFEDALNA TRAAVEEGIV PGGGVTLLRA
ISAVEELIKK LEGDEATGAK IVRRALEEPA RQIAENAGYE GSVIVQQILA ETKNPRYGFN
AATGEFVDMV EAGIVDPAKV TRSALQNAAS IGALILTTEA VVAEKPEKKE STPASAGAGD
MDF
