ID   THSA_SACSH              Reviewed;         560 AA.
AC   P46219;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Thermosome subunit alpha;
DE   AltName: Full=Chaperonin subunit alpha;
DE   AltName: Full=Ring complex subunit alpha;
DE   AltName: Full=Thermophilic factor 55 alpha;
DE            Short=TF55-alpha;
DE   AltName: Full=Thermophilic factor 56;
DE   AltName: Full=Thermosome subunit 1;
GN   Name=thsA; Synonyms=tf56;
OS   Saccharolobus shibatae (Sulfolobus shibatae).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=2286;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12;
RX   PubMed=7473746; DOI=10.1006/jmbi.1995.0585;
RA   Kagawa H.K., Osipiuk J., Maltsev N., Overbeek R., Quaite-Randall E.,
RA   Joachimiak A., Trent J.D.;
RT   "The 60 kDa heat shock proteins in the hyperthermophilic archaeon
RT   Sulfolobus shibatae.";
RL   J. Mol. Biol. 253:712-725(1995).
CC   -!- FUNCTION: Molecular chaperone; binds unfolded polypeptides in vitro,
CC       stimulates protein folding and has ATPase activity.
CC   -!- SUBUNIT: Forms a Heterooligomeric complex of two stacked nine-membered
CC       rings; one of alpha and the other of beta subunits.
CC   -!- INDUCTION: By heat shock.
CC   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR   EMBL; L34691; AAA87624.1; -; Genomic_DNA.
DR   PIR; S59859; S59859.
DR   AlphaFoldDB; P46219; -.
DR   SMR; P46219; -.
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   Stress response.
FT   CHAIN           1..560
FT                   /note="Thermosome subunit alpha"
FT                   /id="PRO_0000128404"
FT   REGION          535..560
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   560 AA;  59703 MW;  F42C945E74565604 CRC64;
     MASPVLLLKE GTSRTTGRDA LRNNILAAKT LAEMLRSSLG PKGLDKMLID SFGDVTITND
     GATIVKDMEI QHPAAKLLVE AAKAQDAEVG DGTTSAVVLA GALLEKAESL LDQNIHPTII
     IEGYKKAYTK ALELLPQLGT RIDIRDLNSS VARDTLRKIA FTTLASKFIA EGAELNKIID
     MVIDAIVNVA EPLPNGGYNV SLDLIKIDKK KGGSIEDSVL VKGLVLDKEV VHPGMPRRVT
     KAKIAVLDAA LEVEKPEISA KISITSPEQI KAFLDEESKY LKDMVDKLAS IGANVVICQK
     GIDDIAQHFL AKKGILAVRR VKRSDIEKLE KALGARIISS IKDATPDDLG YAELVEERRV
     GNDKMVFIEG AKNLKAVNIL LRGSNDMALD EAERSINDAL HALRNILLEP VILPGGGAIE
     LELAMKLREY ARSVGGKEQL AIEAFADALE EIPTILAETA GLEAISALMD LRARHAKGLT
     NTGVDVIGGK IVDDVYALNI IEPIRVKAQV LKSATEAATA ILKIDDLIAA APLKSEKKGG
     EGSKEESGGE GGAGTPSLGD