ID   THS1_HALVD              Reviewed;         560 AA.
AC   O30561; D4GYX9;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Thermosome subunit 1;
DE   AltName: Full=Heat shock protein CCT1;
GN   Name=cct1; OrderedLocusNames=HVO_0133;
OS   Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS   NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=309800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC   STRAIN=DS2 / DSM 5716 / WFD11;
RX   PubMed=9335278; DOI=10.1128/jb.179.20.6318-6324.1997;
RA   Kuo Y.-P., Thompson D.K., St Jean A., Charlebois R.L., Daniels C.J.;
RT   "Characterization of two heat shock genes from Haloferax volcanii: a model
RT   system for transcription regulation in the Archaea.";
RL   J. Bacteriol. 179:6318-6324(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC   B-1768 / DS2;
RX   PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA   Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA   Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA   Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT   "The complete genome sequence of Haloferax volcanii DS2, a model
RT   archaeon.";
RL   PLoS ONE 5:E9605-E9605(2010).
RN   [3]
RP   ATPASE ACTIVITY, SUBUNIT, AND INDUCTION.
RC   STRAIN=DS2 / DS70;
RX   PubMed=12482584; DOI=10.1016/s0014-5793(02)03685-2;
RA   Large A.T., Kovacs E., Lund P.A.;
RT   "Properties of the chaperonin complex from the halophilic archaeon
RT   Haloferax volcanii.";
RL   FEBS Lett. 532:309-312(2002).
RN   [4]
RP   FUNCTION, SUBUNIT, AND ELECTRON MICROSCOPY OF THE THERMOSOME.
RC   STRAIN=DS2 / DS70;
RX   PubMed=16968228; DOI=10.1111/j.1365-2958.2006.05324.x;
RA   Kapatai G., Large A., Benesch J.L., Robinson C.V., Carrascosa J.L.,
RA   Valpuesta J.M., Gowrinathan P., Lund P.A.;
RT   "All three chaperonin genes in the archaeon Haloferax volcanii are
RT   individually dispensable.";
RL   Mol. Microbiol. 61:1583-1597(2006).
CC   -!- FUNCTION: Molecular chaperone that assists in the folding or refolding
CC       of nascent or denatured proteins along with ATP hydrolysis (Probable).
CC       ATPase activity is highest in thermosome assemblies containing
CC       CCT1:CCT2, followed by assemblies containing CCT1:CCT2:CCT3. Required
CC       for thermosome ATPase activity. Not required for growth.
CC       {ECO:0000269|PubMed:16968228, ECO:0000305}.
CC   -!- SUBUNIT: The thermosome or CCT complex is a oligomeric complex of two
CC       octameric double-ring structures; the complex is probably a
CC       heterooligomer of CCT1, CCT2 AND CCT3 with yet unknown stoichiometry.
CC       {ECO:0000269|PubMed:12482584, ECO:0000269|PubMed:16968228}.
CC   -!- INDUCTION: By heat shock (at protein level).
CC       {ECO:0000269|PubMed:12482584, ECO:0000269|PubMed:9335278}.
CC   -!- MISCELLANEOUS: Can substitute for loss of cct2 or cct3. One of either
CC       cct1 or cct2 is required for growth.
CC   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR   EMBL; AF010470; AAB81497.1; -; Genomic_DNA.
DR   EMBL; CP001956; ADE03512.1; -; Genomic_DNA.
DR   PIR; T48841; T48841.
DR   AlphaFoldDB; O30561; -.
DR   SMR; O30561; -.
DR   STRING; 309800.C498_18903; -.
DR   EnsemblBacteria; ADE03512; ADE03512; HVO_0133.
DR   KEGG; hvo:HVO_0133; -.
DR   eggNOG; arCOG01257; Archaea.
DR   HOGENOM; CLU_008891_7_3_2; -.
DR   OMA; HPAANMI; -.
DR   BRENDA; 5.6.1.7; 2561.
DR   Proteomes; UP000008243; 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; Nucleotide-binding; Reference proteome;
KW   Stress response.
FT   CHAIN           1..560
FT                   /note="Thermosome subunit 1"
FT                   /id="PRO_0000128387"
FT   REGION          525..550
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   560 AA;  58925 MW;  88B73B2AD70DC341 CRC64;
     MSQRMQQGQP MIILGEDSQR TSGQDAQSMN ITAGKAVAEA VRTTLGPKGM DKMLVDSGGQ
     VVVTNDGVTI LKEMDIDHPA ANMIVEVSET QEDEVGDGTT TAVINAGELL DQAEDLLDSD
     VHATTIAQGY RQAAEKAKEV LEDNAIEVTE DDRETLTKIA ATAMTGKGAE SAKDLLSELV
     VDAVLAVKDD DGIDTNNVSI EKVVGGTIDN SELVEGVIVD KERVDENMPY AVEDANIAIL
     DDALEVRETE IDAEVNVTDP DQLQQFLDQE EKQLKEMVDQ LVEVGADAVF VGDGIDDMAQ
     HYLAKEGILA VRRAKSSDLK RLARATGGRV VSSLDDIEAD DLGFAGSVGQ KDVGGDERIF
     VEDVEDAKSV TLILRGGTEH VVDELERAIE DSLGVVRTTL EDGKVLPGGG APETELSLQL
     REFADSVGGR EQLAVEAFAE ALDIIPRTLA ENAGLDPIDS LVDLRSRHDG GEFAAGLDAY
     TGEVIDMEEE GVVEPLRVKT QAIESATEAA VMILRIDDVI AAGDLSGGQT GSDDDDGGAP
     GGMGGGMGGM GGMGGMGGAM