ID   THSG_SACSH              Reviewed;         535 AA.
AC   Q9HH21; Q9V2T6;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Thermosome subunit gamma;
DE   AltName: Full=Chaperonin subunit gamma;
DE   AltName: Full=HSP60 gamma subunit;
DE   AltName: Full=Thermophilic factor 55 gamma;
DE            Short=TF55-gamma;
DE   AltName: Full=Thermosome subunit 3;
GN   Name=thsC; Synonyms=thsG;
OS   Saccharolobus shibatae (Sulfolobus shibatae).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=2286;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12;
RA   Yaoi T., Trent J.D.;
RT   "Sulfolobus shibatae HSP60 gamma subunit.";
RL   Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 90-401.
RX   PubMed=10508614; DOI=10.1016/s0960-9822(99)80457-6;
RA   Archibald J.M., Logsdon J.M. Jr., Doolittle W.F.;
RT   "Recurrent paralogy in the evolution of archaeal chaperonins.";
RL   Curr. Biol. 9:1053-1056(1999).
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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR   EMBL; AF313410; AAG37273.1; -; Genomic_DNA.
DR   EMBL; AF149922; AAF03363.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9HH21; -.
DR   SMR; Q9HH21; -.
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.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Nucleotide-binding.
FT   CHAIN           1..535
FT                   /note="Thermosome subunit gamma"
FT                   /id="PRO_0000128406"
SQ   SEQUENCE   535 AA;  58538 MW;  813916E2BCD8B9CB CRC64;
     MAYLLREGTQ RSTGNEVILN NIAVAKILLE MLKSSLGPKG LDKMLVEGQD ITITNDGATI
     VKNMEVQHPT AKLLIETAKT VDTEVGDGTT SVVVLAGLLL EKAEDLLNQK IHPTVIIEGY
     RKALSSSLEL LKSIADKISP EDRKIVHDLV YTTLSSKFFS TEHTLEKIIN LVIEASLAVL
     DKRDGTYDLD IKNIKIVKVN GGEFDDSELV NGIVVDKEPT NENMPKRAEN VKVMLADFPL
     KLEKTEISMK LGISDPTQIK GYLDEQTAYV KQMVDKIKAM GVKLFITQKD IDEVASYLMG
     KSGIIALKNV KRSDIELLSR ATGAKIASSM KDANESDLGE AKLVEVRNLG KNKYLFIQSD
     KAKAVTVIIK GSNNMVTDEA ERSLNDAFNS IRNLLLEPYI VAGGGAVEEE LAKRLRENAG
     KVPGKEQLAF NAFADALEEY VSILSETAGM DPISALTEIR HKHANGLKNA GIDIVKARIY
     DNMLELKVID SLKVKEQVLK SATEAATAIL KIDDMIAAAP AKQQPQPQQP NPYLG