CH60_THET2
ID CH60_THET2 Reviewed; 543 AA.
AC P61490; P45746; Q60018; Q9RA44;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 109.
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, groE, groL {ECO:0000255|HAMAP-Rule:MF_00600}, hsp60, mopA;
GN OrderedLocusNames=TT_C1714;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Boskocik J., Moreno R., Valpuesta J.M., Berenguer J.;
RT "Characterization of the cpn10-cpn60 chaperonine from Thermus thermophilus
RT HB27.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), AND SUBUNIT.
RX PubMed=15296740; DOI=10.1016/j.str.2004.05.020;
RA Shimamura T., Koike-Takeshita A., Yokoyama K., Masui R., Murai N.,
RA Yoshida M., Taguchi H., Iwata S.;
RT "Crystal structure of the native chaperonin complex from Thermus
RT thermophilus revealed unexpected asymmetry at the cis-cavity.";
RL Structure 12:1471-1480(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, ECO:0000269|PubMed:15296740}.
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; AJ250409; CAB65482.1; -; Genomic_DNA.
DR EMBL; AE017221; AAS82056.1; -; Genomic_DNA.
DR RefSeq; WP_011174077.1; NC_005835.1.
DR PDB; 4V4O; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/a/b/c/d/e/f/g/h/i/j/k/l/m/n=1-543.
DR PDBsum; 4V4O; -.
DR AlphaFoldDB; P61490; -.
DR SMR; P61490; -.
DR STRING; 262724.TT_C1714; -.
DR PRIDE; P61490; -.
DR EnsemblBacteria; AAS82056; AAS82056; TT_C1714.
DR GeneID; 3168209; -.
DR KEGG; tth:TT_C1714; -.
DR eggNOG; COG0459; Bacteria.
DR HOGENOM; CLU_016503_3_0_0; -.
DR OMA; TDTDKME; -.
DR OrthoDB; 265347at2; -.
DR EvolutionaryTrace; P61490; -.
DR Proteomes; UP000000592; 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 3D-structure; ATP-binding; Chaperone; Cytoplasm; Isomerase;
KW Nucleotide-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..543
FT /note="Chaperonin GroEL"
FT /id="PRO_0000063581"
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 133
FT /note="L -> P (in Ref. 1; CAB65482)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="E -> K (in Ref. 1; CAB65482)"
FT /evidence="ECO:0000305"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:4V4O"
FT HELIX 8..26
FT /evidence="ECO:0007829|PDB:4V4O"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:4V4O"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:4V4O"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:4V4O"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:4V4O"
FT HELIX 52..58
FT /evidence="ECO:0007829|PDB:4V4O"
FT HELIX 64..84
FT /evidence="ECO:0007829|PDB:4V4O"
FT HELIX 88..107
FT /evidence="ECO:0007829|PDB:4V4O"
FT HELIX 112..132
FT /evidence="ECO:0007829|PDB:4V4O"
FT HELIX 140..151
FT /evidence="ECO:0007829|PDB:4V4O"
FT HELIX 154..165
FT /evidence="ECO:0007829|PDB:4V4O"
FT STRAND 171..177
FT /evidence="ECO:0007829|PDB:4V4O"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:4V4O"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:4V4O"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:4V4O"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:4V4O"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:4V4O"
FT TURN 206..209
FT /evidence="ECO:0007829|PDB:4V4O"
FT STRAND 213..223
FT /evidence="ECO:0007829|PDB:4V4O"
FT HELIX 228..239
FT /evidence="ECO:0007829|PDB:4V4O"
FT STRAND 245..250
FT /evidence="ECO:0007829|PDB:4V4O"
FT HELIX 254..266
FT /evidence="ECO:0007829|PDB:4V4O"
FT STRAND 271..275
FT /evidence="ECO:0007829|PDB:4V4O"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:4V4O"
FT HELIX 280..294
FT /evidence="ECO:0007829|PDB:4V4O"
FT TURN 301..303
FT /evidence="ECO:0007829|PDB:4V4O"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:4V4O"
FT HELIX 312..314
FT /evidence="ECO:0007829|PDB:4V4O"
FT STRAND 316..323
FT /evidence="ECO:0007829|PDB:4V4O"
FT STRAND 328..333
FT /evidence="ECO:0007829|PDB:4V4O"
FT HELIX 337..351
FT /evidence="ECO:0007829|PDB:4V4O"
FT HELIX 357..370
FT /evidence="ECO:0007829|PDB:4V4O"
FT STRAND 374..379
FT /evidence="ECO:0007829|PDB:4V4O"
FT HELIX 384..407
FT /evidence="ECO:0007829|PDB:4V4O"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:4V4O"
FT TURN 412..414
FT /evidence="ECO:0007829|PDB:4V4O"
FT HELIX 415..428
FT /evidence="ECO:0007829|PDB:4V4O"
FT HELIX 433..445
FT /evidence="ECO:0007829|PDB:4V4O"
FT HELIX 448..456
FT /evidence="ECO:0007829|PDB:4V4O"
FT HELIX 461..470
FT /evidence="ECO:0007829|PDB:4V4O"
FT STRAND 477..479
FT /evidence="ECO:0007829|PDB:4V4O"
FT TURN 481..483
FT /evidence="ECO:0007829|PDB:4V4O"
FT STRAND 486..488
FT /evidence="ECO:0007829|PDB:4V4O"
FT TURN 489..493
FT /evidence="ECO:0007829|PDB:4V4O"
FT STRAND 495..497
FT /evidence="ECO:0007829|PDB:4V4O"
FT HELIX 498..516
FT /evidence="ECO:0007829|PDB:4V4O"
FT STRAND 518..524
FT /evidence="ECO:0007829|PDB:4V4O"
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
