ID   THS_DESSY               Reviewed;         545 AA.
AC   Q53546;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Thermosome subunit;
DE   AltName: Full=Hyperthermophilic heat shock protein;
DE            Short=HHSP;
GN   Name=ths;
OS   Desulfurococcus sp. (strain SY).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Desulfurococcus; unclassified Desulfurococcus.
OX   NCBI_TaxID=59822;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7677788; DOI=10.1006/bbrc.1995.2346;
RA   Kagawa Y., Ohta T., Abe Y., Endo H., Yohda M., Kato N., Endo I.,
RA   Hamamoto T., Ichida M., Hoaki T.;
RT   "Gene of heat shock protein of sulfur-dependent archaeal hyperthermophile
RT   Desulfurococcus.";
RL   Biochem. Biophys. Res. Commun. 214:730-736(1995).
CC   -!- FUNCTION: Molecular chaperone; binds unfolded polypeptides in vitro,
CC       and has a weak ATPase activity. {ECO:0000250}.
CC   -!- SUBUNIT: Forms an oligomeric complex of eight-membered rings.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR   EMBL; S79557; AAB35235.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q53546; -.
DR   SMR; Q53546; -.
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; Stress response.
FT   CHAIN           1..545
FT                   /note="Thermosome subunit"
FT                   /id="PRO_0000128384"
SQ   SEQUENCE   545 AA;  59138 MW;  97878CA449D0F612 CRC64;
     MAQLAGQPVV ILPEGTQRYV GRDAQRLNIL AARIVAETIR TTLGPKGMDK MLVDSLGDIV
     ITNDGATILD EMDIQHPAAK MMVEVAKTQD KEAGDGTTTA VVIAGELLKK AEELLDQNIH
     PSIIIKGYAL AAEKAQEILE GIAKEVSPDD VETLKKAAVT SITGKAAEEE REYLAEIAVE
     AVRQVAEKVG DKYKVDLDNI KFEKKEGASV HETQLIRGVV IDKEVVHPGM PKRVENAKIA
     LINDALEVKE TETDAEIRIT SPEQLQAFLE QEERMLREMV DKIKEVGANV VFVQKGIDDL
     AQHYLAKYGI MAVRRVKKSD MEKLAKATGA KIVTNVRDLT PEDLGEAELV EQRKVAGENM
     IFVEGCKNPK AVTILIRGGT EHVVDEVERA LEDAVKVVKD IVEDGKILPA GGAPEIELAI
     KLDEYAKEVG GKEQLAIEAF AEALKVIPRT LAENAGLDPV ETLVKVIAAH KEKGPTIGVD
     VFEGEPADMM EKGVIAPLRV PKQAIKSASE AAIMILRIDD VIAASKLEKD KEDKGGSNDF
     GSDLD