ID   THSB_THEK1              Reviewed;         546 AA.
AC   O24730;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2001, sequence version 2.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Thermosome subunit beta;
DE   AltName: Full=Chaperonin subunit beta;
DE   AltName: Full=Thermosome subunit 2;
GN   Name=thsB;
OS   Thermococcus sp. (strain JCM 11816 / KS-1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus; unclassified Thermococcus.
OX   NCBI_TaxID=1295125;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9356252; DOI=10.1006/jmbi.1997.1337;
RA   Yoshida T., Yohda M., Iida T., Maruyama T., Taguchi H., Yazaki K., Ohta T.,
RA   Odaka M., Endo I., Kagawa Y.;
RT   "Structural and functional characterization of homo-oligomeric complexes of
RT   alpha and beta chaperonin subunits from the hyperthermophilic archaeum
RT   Thermococcus strain KS-1.";
RL   J. Mol. Biol. 273:635-645(1997).
RN   [2]
RP   SEQUENCE REVISION TO 325; 509 AND 538.
RA   Yohda M.;
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Molecular chaperone; binds unfolded polypeptides in vitro,
CC       and has a weak ATPase activity. {ECO:0000250}.
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; AB001081; BAA22208.2; -; Genomic_DNA.
DR   AlphaFoldDB; O24730; -.
DR   SMR; O24730; -.
DR   BRENDA; 3.6.4.B10; 6304.
DR   BRENDA; 5.6.1.7; 6304.
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; IEA:InterPro.
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.
FT   CHAIN           1..546
FT                   /note="Thermosome subunit beta"
FT                   /id="PRO_0000128412"
SQ   SEQUENCE   546 AA;  59174 MW;  DC79F1077CA5EE12 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 GGAPEIELSI
     RLDEYAKEVG GKEQLAIEAF AEALKVIPRT LAENAGLDPI ETLVKVIAAH KEKGPTIGVD
     VFEGEPADML ERGVIAPVRV PKQAIKSASE AAIMILRIDD VIAASKLEKD KEGGKGGSED
     FGSDLD