ID   THS2_HALVD              Reviewed;         557 AA.
AC   O30560; D4GRZ6;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Thermosome subunit 2;
DE   AltName: Full=Heat shock protein CCT2;
GN   Name=cct2; OrderedLocusNames=HVO_0455;
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. Seems to
CC       contribute to 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: One of either CCT1 or CCT2 is required for growth.
CC   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR   EMBL; AF010469; AAB81496.1; -; Genomic_DNA.
DR   EMBL; CP001956; ADE03416.1; -; Genomic_DNA.
DR   PIR; T47128; T47128.
DR   AlphaFoldDB; O30560; -.
DR   SMR; O30560; -.
DR   IntAct; O30560; 16.
DR   STRING; 309800.C498_16404; -.
DR   EnsemblBacteria; ADE03416; ADE03416; HVO_0455.
DR   KEGG; hvo:HVO_0455; -.
DR   eggNOG; arCOG01257; Archaea.
DR   HOGENOM; CLU_008891_7_3_2; -.
DR   OMA; QTGSNDM; -.
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..557
FT                   /note="Thermosome subunit 2"
FT                   /id="PRO_0000128388"
FT   REGION          527..557
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   557 AA;  59298 MW;  5607A4591DBEF3A4 CRC64;
     MSQRMQQGQP MIIMGEDAQR VKDRDAQEYN IRAARAVAEA VRSTLGPKGM DKMLVDSMGD
     VTITNDGVTI LKEMDIDNPT AEMIVEVAET QEDEAGDGTT TAVAIAGELL KNAEDLLEQD
     IHPTAIIRGF NLASEKAREE IDDIAERVDP DDEELLKKVA ETSMTGKSSE LNKELLADLI
     VRAVRQVTVE ANDGSHVVDL ENVSIETQTG RSASESELLT GAVIDKDPVH DDMPVQFDEA
     DVLLLNEPVE VEETDIDTNV SIESPDQLQK FLDQEEAQLK QKVDQIVDSG ADVVFCQKGI
     DDLAQHYLAK QGILAVRRTK KSDIRFLKNI TGAAVVSDLD SIEAAVLGRA SVRRDEAGEL
     FYVEGIGDDV HGVTLLLRGS TDHVVDELER GVQDALDVVA STVADGRVLA GGGAIEVELA
     SRLRNYADSV SGREQLAVEA YADALELVPR VLAENAGLDS IDTLVDLRAA HEDGQVRAGL
     NVFTGEVEDA FDAGVVETAH AKEQAVASAS EAANLVLKID DIIAAGDLST GGDDDEEGGA
     PGGMGGMGGM GGMGGAM