ID   THSB_THEKO              Reviewed;         546 AA.
AC   Q52500;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Thermosome subunit beta;
DE   AltName: Full=Chaperonin subunit beta;
DE   AltName: Full=Thermosome subunit 2;
GN   Name=thsB; Synonyms=cpkB, ths; OrderedLocusNames=TK2303;
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=9023959; DOI=10.1128/aem.63.2.785-789.1997;
RA   Yan Z., Fujiwara S., Kohda K., Takagi M., Imanaka T.;
RT   "In vitro stabilization and in vivo solubilization of foreign proteins by
RT   the beta subunit of a chaperonin from the hyperthermophilic archaeon
RT   Pyrococcus sp. strain KOD1.";
RL   Appl. Environ. Microbiol. 63:785-789(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
CC   -!- FUNCTION: Molecular chaperone; binds unfolded polypeptides in vitro,
CC       and has a weak ATPase activity.
CC   -!- SUBUNIT: Forms a Heterooligomeric complex of two stacked eight-membered
CC       rings. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR   EMBL; D29672; BAA06143.1; -; Genomic_DNA.
DR   EMBL; AP006878; BAD86492.1; -; Genomic_DNA.
DR   PIR; S61294; S61294.
DR   RefSeq; WP_011251253.1; NC_006624.1.
DR   AlphaFoldDB; Q52500; -.
DR   SMR; Q52500; -.
DR   IntAct; Q52500; 1.
DR   MINT; Q52500; -.
DR   STRING; 69014.TK2303; -.
DR   EnsemblBacteria; BAD86492; BAD86492; TK2303.
DR   GeneID; 3233720; -.
DR   KEGG; tko:TK2303; -.
DR   PATRIC; fig|69014.16.peg.2258; -.
DR   eggNOG; arCOG01257; Archaea.
DR   HOGENOM; CLU_008891_7_3_2; -.
DR   InParanoid; Q52500; -.
DR   OMA; HPAANMI; -.
DR   OrthoDB; 11742at2157; -.
DR   PhylomeDB; Q52500; -.
DR   BRENDA; 3.6.4.B10; 5246.
DR   Proteomes; UP000000536; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   CDD; cd03343; cpn60; 1.
DR   Gene3D; 1.10.560.10; -; 1.
DR   Gene3D; 3.30.260.10; -; 1.
DR   Gene3D; 3.50.7.10; -; 1.
DR   InterPro; IPR017998; Chaperone_TCP-1.
DR   InterPro; IPR002194; Chaperonin_TCP-1_CS.
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   InterPro; IPR012714; Thermosome_arc.
DR   PANTHER; PTHR11353; PTHR11353; 1.
DR   Pfam; PF00118; Cpn60_TCP1; 1.
DR   PRINTS; PR00304; TCOMPLEXTCP1.
DR   SUPFAM; SSF48592; SSF48592; 1.
DR   SUPFAM; SSF52029; SSF52029; 1.
DR   SUPFAM; SSF54849; SSF54849; 1.
DR   TIGRFAMs; TIGR02339; thermosome_arch; 1.
DR   PROSITE; PS00750; TCP1_1; 1.
DR   PROSITE; PS00751; TCP1_2; 1.
DR   PROSITE; PS00995; TCP1_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..546
FT                   /note="Thermosome subunit beta"
FT                   /id="PRO_0000128411"
SQ   SEQUENCE   546 AA;  59158 MW;  866191077CBD8E18 CRC64;
     MAQLAGQPVV ILPEGTQRYV GRDAQRLNIL AARIIAETVR TTLGPKGMDK MLVDSLGDIV
     ITNDGATILD EMDIQHPAAK MMVEVAKTQD KEAGDGTTTA VVIAGELLRK AEELLDQNIH
     PSIIIKGYAL AAEKAQEILD EIAKDVDVED REILKKAAVT SITGKAAEEE REYLAEIAVE
     AVKQVAEKVG ETYKVDLDNI KFEKKEGGSV KDTQLIKGVV IDKEVVHPGM PKRVEGAKIA
     LINEALEVKE TETDAEIRIT SPEQLQAFLE QEEKMLREMV DKIKEVGANV VFVQKGIDDL
     AQHYLAKYGI MAVRRVKKSD MEKLAKATGA KIVTNVRDLT PEDLGEAELV EQRKVAGENM
     IFVEGCKNPK AVTILIRGGT EHVVDEVERA LEDAVKVVKD IVEDGKIVAA GGAPEIELAI
     RLDEYAKEVG GKEQLAIEAF AEALKVIPRT LAENAGLDPI ETLVKVIAAH KEKGPTIGVD
     VFEGEPADML ERGVIAPVRV PKQAIKSASE AAIMILRIDD VIAASKLEKD KEGGKGGSED
     FGSDLD