ID   THS_PYRHO               Reviewed;         549 AA.
AC   O57762;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Thermosome subunit;
DE   AltName: Full=Chaperonin subunit;
GN   Name=ths; OrderedLocusNames=PH0017;
OS   Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS   100139 / OT-3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=70601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX   PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA   Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA   Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA   Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA   Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA   Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT   "Complete sequence and gene organization of the genome of a hyper-
RT   thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL   DNA Res. 5:55-76(1998).
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; BA000001; BAA29085.1; -; Genomic_DNA.
DR   PIR; F71219; F71219.
DR   RefSeq; WP_010884137.1; NC_000961.1.
DR   AlphaFoldDB; O57762; -.
DR   SMR; O57762; -.
DR   DIP; DIP-29172N; -.
DR   IntAct; O57762; 2.
DR   MINT; O57762; -.
DR   STRING; 70601.3256402; -.
DR   EnsemblBacteria; BAA29085; BAA29085; BAA29085.
DR   GeneID; 1443919; -.
DR   KEGG; pho:PH0017; -.
DR   eggNOG; arCOG01257; Archaea.
DR   OMA; HPAANMI; -.
DR   OrthoDB; 11742at2157; -.
DR   BRENDA; 3.6.4.B10; 5244.
DR   Proteomes; UP000000752; 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; 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..549
FT                   /note="Thermosome subunit"
FT                   /id="PRO_0000128396"
FT   REGION          528..549
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   549 AA;  59693 MW;  9A451CA8C6CFEB4D CRC64;
     MAQLAGQPIL ILPEGTQRYV GRDAQRMNIL AARIIAETVR TTLGPKGMDK MLVDSLGDIV
     ITNDGATILD EMDIQHPAAK MMVEVAKTQD KEAGDGTTTA VVIAGELLKK AEELLDQNIH
     PSIIIKGYTL ASQKAQEILD SIAKEVKPDD EEVLLKAAMT AITGKAAEEE REYLAKLAVE
     AVKLVAEEKD GKLKVDIDNI KLEKKEGGAV RDTRLIRGVV IDKEVVHPGM PKRIENAKIA
     LINDALEVKE TETDAEIRIT SPEQLQAFLE QEEKMLKEMV DKIKEVGANV VFVQKGIDDL
     AQHYLAKYGI LAVRRVKKSD MEKLAKATGA KIVTNIRDLT PEDLGEAELV EERKVAGENM
     IFVEGCKNPK AVTILIRGGT EHVVDEVERA LEDAIKVVKD ILEDGKIIAG GGASEIELSI
     KLDEYAKEVG GKEQLAIEAF AEALKVIPRT LAENAGLDPI ETLVKVIAAH KEKGQTIGID
     VYEGEPADMM ERGVIEPVRV KKQAIKSASE AAIMILRIDD VIAASKLEKE KEGEKGGGSE
     EFSGSSDLD