ID   THSB_THEK8              Reviewed;         545 AA.
AC   O24732;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 83.
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 KS-8).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus; unclassified Thermococcus.
OX   NCBI_TaxID=79680;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Yoshida T., Yohda M., Ohta T., Iida T., Maruyama T., Kagawa Y.;
RL   Submitted (SEP-1997) 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; AB001083; BAA22210.1; -; Genomic_DNA.
DR   AlphaFoldDB; O24732; -.
DR   SMR; O24732; -.
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..545
FT                   /note="Thermosome subunit beta"
FT                   /id="PRO_0000128414"
SQ   SEQUENCE   545 AA;  59067 MW;  F80B575916DFE1F3 CRC64;
     MAQLAGQPVV ILPEGTQRYV GRDAQRLNIL AARIIAETVR TTLGPKGMDK MLVDSLGDIV
     ITNDGATILD EMDIQHPAAK MMVEVAKTQD KEAGDGTTTA VVIAGELLRK AEELLDQNIH
     PSIIIKGYAL AAEKAQEILD SIARDVDVED REILKKAAMT AITGKAAEEE REYLAEIAVE
     AVKQVAEKVG DRYHVDLDNI KFEKKEGGSV KDTQLIKGVV IDKEVVHPGM RKRVEGAKIA
     LINEALEVKE TETDAEIRIT SPEQLQAFLE QEEKMLREMV DKIKEVGANV VFVQKGIDDL
     AQHYLAKYGI MAVRRVKKSD MEKLAKATGA KIVTNVRDLT PEDLGEAELV EQRKVAGENM
     IFVEGCKNPK AVTILIRGGT EHVVDEVERA LEDAVKVVKD IVEDGKIVAA GGAPEIELAI
     SVDEYAKEVG GKEQLAIEAF AEALKVIPRT LAGNAGLDPI ETLVKVIAAH KEKGPTIGVD
     VFEGEPADML ERGVIAPVRV PKQAIKSAKA AIMILRIDDV IAASKLEKDK EGGKGGTRDF
     GSDLD