ID   THSA_SULTO              Reviewed;         559 AA.
AC   O24734; F9VNY9;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Thermosome subunit alpha;
DE   AltName: Full=Chaperonin subunit alpha;
DE   AltName: Full=Thermosome subunit 1;
GN   Name=thsA; OrderedLocusNames=STK_12530;
OS   Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS   (Sulfolobus tokodaii).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfurisphaera.
OX   NCBI_TaxID=273063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 183-202 AND
RP   221-235.
RC   STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX   PubMed=9245723; DOI=10.1006/bbrc.1997.6916;
RA   Nakamura N., Taguchi H., Ishii N., Yoshida M., Suzuki M., Endo I.,
RA   Miura K., Yohda M.;
RT   "Purification and molecular cloning of the group II chaperonin from the
RT   acidothermophilic archaeon, Sulfolobus sp. strain 7.";
RL   Biochem. Biophys. Res. Commun. 236:727-732(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX   PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA   Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA   Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA   Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA   Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT   "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT   Sulfolobus tokodaii strain7.";
RL   DNA Res. 8:123-140(2001).
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 nine-membered
CC       rings; one of alpha and the other of beta subunits. {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; AB001085; BAA22212.1; -; Genomic_DNA.
DR   EMBL; BA000023; BAK54497.1; -; Genomic_DNA.
DR   PIR; JC5616; JC5616.
DR   RefSeq; WP_052846517.1; NC_003106.2.
DR   AlphaFoldDB; O24734; -.
DR   SMR; O24734; -.
DR   STRING; 273063.STK_12530; -.
DR   EnsemblBacteria; BAK54497; BAK54497; STK_12530.
DR   GeneID; 1459250; -.
DR   KEGG; sto:STK_12530; -.
DR   PATRIC; fig|273063.9.peg.1411; -.
DR   eggNOG; arCOG01257; Archaea.
DR   OMA; QTGSNDM; -.
DR   OrthoDB; 11742at2157; -.
DR   BRENDA; 5.6.1.7; 15396.
DR   Proteomes; UP000001015; 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   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Direct protein sequencing; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..559
FT                   /note="Thermosome subunit alpha"
FT                   /id="PRO_0000128407"
FT   REGION          536..559
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        536..552
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   559 AA;  60169 MW;  7726247E2C31858D CRC64;
     MANAPVLLLK EGTQRSSGRD ALKNNILAAV TLAEMLKSSL GPRGLDKMLI DSFGDVTITN
     DGATIVKEME IQHPAAKLLV EAAKAQDAEV GDGTTSAVVL AGLLLDKADD LLDQNIHPTI
     IIEGYKKALN KSLEIIDQLA TKIDVSNLNS LATRDQLKKI VYTTMSSKFI AGGEEMDKIM
     NMVIDAVSIV AEPLPEGGYN VPLDLIKIDK KKGGSIEDSM LVHGLVLDKE VVHPGMPRRV
     EKAKIAVLDA ALEVEKPEIS AKISITSPEQ IKAFLDEEAK YLKDMVDKLA SIGANVVICQ
     KGIDDVAQHF LAKKGILAVR RVKRSDIEKL EKALGARIIS SIKDATPEDL GYAELVEERR
     VGNDKMVFIE GAKNPKAVNI LLRGSNDMAL DEAERSINDA LHSLRNVLMK PMIVAGGGAV
     ETELALRLRE YARSVGGKEQ LAIEKFAEAL EEIPMILAET AGMEPIQTLM DLRAKHAKGL
     INAGVDVMNG KIADDMLALN VLEPVRVKAQ VLKSAVEAAT AILKIDDLIA AAPLKSGEKK
     GEKKEGGEEE KSSTPSSLE