ID   THS_PYRAB               Reviewed;         550 AA.
AC   Q9V2Q7; G8ZFJ5;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Thermosome subunit;
DE   AltName: Full=Chaperonin subunit;
GN   Name=ths; Synonyms=thsA; OrderedLocusNames=PYRAB00180; ORFNames=PAB2341;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ248283; CAB48941.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE69386.1; -; Genomic_DNA.
DR   PIR; F75186; F75186.
DR   RefSeq; WP_010867141.1; NC_000868.1.
DR   AlphaFoldDB; Q9V2Q7; -.
DR   SMR; Q9V2Q7; -.
DR   STRING; 272844.PAB2341; -.
DR   EnsemblBacteria; CAB48941; CAB48941; PAB2341.
DR   GeneID; 1495702; -.
DR   KEGG; pab:PAB2341; -.
DR   PATRIC; fig|272844.11.peg.20; -.
DR   eggNOG; arCOG01257; Archaea.
DR   HOGENOM; CLU_008891_7_3_2; -.
DR   OMA; HPAANMI; -.
DR   OrthoDB; 11742at2157; -.
DR   PhylomeDB; Q9V2Q7; -.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; 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..550
FT                   /note="Thermosome subunit"
FT                   /id="PRO_0000128395"
FT   REGION          529..550
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   550 AA;  59718 MW;  523196D4BB2BAC53 CRC64;
     MAQLAGQPIL ILPEGTQRYV GRDAQRMNIL AARIIAETVR TTLGPKGMDK MLVDSLGDIV
     ITNDGATILD EMDIQHPAAK MMVEVAKTQD KEAGDGTTTA VVIAGELLKK AEELLDQNIH
     PSIVIKGYML AAEKAQEILD SIAKEVKPDD EEVLLKAAMT AITGKAAEEE REYLAKLAVE
     AVKLVAEEKD GKFKVDIDNI KFEKKEGGAV SDTKLIRGVV IDKEVVHPGM PKRVEKAKIA
     LINDALEVKE TETDAEIRIT SPEQLQAFLE QEEKMLKEMV DKIKEVGANV VFVQKGIDDL
     AQHYLAKYGI LAVRRVKKSD MEKLAKATGA KIVTNIRDLT PEDLGEAELV EERKVAGENM
     IFVEGCKNPK AVTILIRGGT EHVVDEVERA LEDAVKVVKD ILEDGKIIAG GGAAEIELSI
     KLDEYAKEVG GKEQLAIEAF AEALKVIPRT LAENAGLDPI ETLVKVIAAH KEKGPTIGID
     VYEGEPADMM ERGVIEPVRV KKQAIKSASE AAIMILRIDD VIAAQKLEKE KEGEKGGGGS
     EDFSSSSDLD