THS3_HALVD
ID THS3_HALVD Reviewed; 524 AA.
AC Q9HHA2; D4GTT3; O31124;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Thermosome subunit 3;
DE AltName: Full=Heat shock protein CCT3;
GN Name=cct3; OrderedLocusNames=HVO_0778;
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], 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 [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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-54.
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=9489666; DOI=10.1046/j.1365-2958.1998.00698.x;
RA Thompson D.K., Daniels C.J.;
RT "Heat shock inducibility of an archaeal TATA-like promoter is controlled by
RT adjacent sequence elements.";
RL Mol. Microbiol. 27:541-551(1998).
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. Not
CC required 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}.
CC -!- MISCELLANEOUS: Cannot be stably overexpressed.
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC38171.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF298660; AAG17906.1; -; Genomic_DNA.
DR EMBL; CP001956; ADE03673.1; -; Genomic_DNA.
DR EMBL; AF029873; AAC38171.1; ALT_FRAME; Genomic_DNA.
DR AlphaFoldDB; Q9HHA2; -.
DR SMR; Q9HHA2; -.
DR IntAct; Q9HHA2; 14.
DR STRING; 309800.C498_14843; -.
DR EnsemblBacteria; ADE03673; ADE03673; HVO_0778.
DR KEGG; hvo:HVO_0778; -.
DR eggNOG; arCOG01257; Archaea.
DR HOGENOM; CLU_008891_7_3_2; -.
DR OMA; YCTGGEI; -.
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..524
FT /note="Thermosome subunit 3"
FT /id="PRO_0000128389"
FT CONFLICT 368
FT /note="R -> K (in Ref. 1; AAG17906)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="D -> Y (in Ref. 1; AAG17906)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 524 AA; 55242 MW; 25E1F4BD49CD8762 CRC64;
MASRMQQPLY ILAEGTNRTH GRSAQDSNIR AGKAVAEAVR TTLGPRGMDK MLVDSSGEVV
ITNDGATILE KMDIEHPAAQ MLVEVSQTQE EEVGDGTTTA AVLTGELLAH AEDLLDDDLH
PTVIVEGYTE AARIAQDAID DMVLDVTLDD DLLRKVAESS MTGKGTGDVT ADVLAKHVVK
AVQMVHEDDN GVFHRDDVRV LTRTGASSSA TELVEGVVLD KEPVNENMPR SVSDATVAVL
DMKLDVRKSE VDTEYNITSV DQLTAAIDAE DSELRGYAKA LADAGVDVVF CTKSIDDRVA
GFLADAGILA FKSVKKSDAR ALARATGAKR LGSLSDLDES DLGRVDAVSI RSFGDDDLAF
VEGGAAARAV TLFLRGGTEH VVDELERAIE DAVDVVVAAI DKGGVVPGAG ATEIAIADRI
RSEAAGIEGR KQLAVEAYAD AVEALPRTLA ENTGMDPIDA LVDLRARYET EGLAGIISSG
RSGEIGDPVE LGVIDPVAVK REAIESATEA ATMIVRIDDV IAAK
