THSA_SACS2
ID THSA_SACS2 Reviewed; 559 AA.
AC Q9V2S9;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Thermosome subunit alpha;
DE AltName: Full=Chaperonin subunit alpha;
DE AltName: Full=Thermophilic factor 55 alpha;
DE Short=TF55-alpha;
DE AltName: Full=Thermosome subunit 1;
GN Name=thsA; OrderedLocusNames=SSO0862;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
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 eight-membered
CC rings. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9V2S9; Q9V2T8: thsB; NbExp=7; IntAct=EBI-16195227, EBI-16195251;
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR EMBL; AF181261; AAD56682.1; -; Genomic_DNA.
DR EMBL; AE006641; AAK41152.1; -; Genomic_DNA.
DR PIR; A99237; A99237.
DR RefSeq; WP_009992283.1; NC_002754.1.
DR PDB; 4XCG; X-ray; 3.74 A; A=1-559.
DR PDB; 4XCI; X-ray; 3.00 A; A=1-559.
DR PDBsum; 4XCG; -.
DR PDBsum; 4XCI; -.
DR AlphaFoldDB; Q9V2S9; -.
DR SMR; Q9V2S9; -.
DR DIP; DIP-61906N; -.
DR IntAct; Q9V2S9; 2.
DR STRING; 273057.SSO0862; -.
DR EnsemblBacteria; AAK41152; AAK41152; SSO0862.
DR GeneID; 44129799; -.
DR KEGG; sso:SSO0862; -.
DR PATRIC; fig|273057.12.peg.873; -.
DR eggNOG; arCOG01257; Archaea.
DR HOGENOM; CLU_008891_7_3_2; -.
DR InParanoid; Q9V2S9; -.
DR OMA; QTGSNDM; -.
DR PhylomeDB; Q9V2S9; -.
DR Proteomes; UP000001974; 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; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
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 3D-structure; ATP-binding; Chaperone; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..559
FT /note="Thermosome subunit alpha"
FT /id="PRO_0000128401"
FT REGION 535..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 30
FT /note="T -> A (in Ref. 1; AAD56682)"
FT /evidence="ECO:0000305"
FT CONFLICT 34
FT /note="M -> R (in Ref. 1; AAD56682)"
FT /evidence="ECO:0000305"
FT HELIX 19..36
FT /evidence="ECO:0007829|PDB:4XCI"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:4XCI"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:4XCI"
FT HELIX 61..67
FT /evidence="ECO:0007829|PDB:4XCI"
FT HELIX 73..88
FT /evidence="ECO:0007829|PDB:4XCI"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:4XCI"
FT HELIX 93..112
FT /evidence="ECO:0007829|PDB:4XCI"
FT HELIX 117..138
FT /evidence="ECO:0007829|PDB:4XCI"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:4XCI"
FT HELIX 154..164
FT /evidence="ECO:0007829|PDB:4XCI"
FT HELIX 179..187
FT /evidence="ECO:0007829|PDB:4XCI"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:4XCI"
FT HELIX 396..408
FT /evidence="ECO:0007829|PDB:4XCI"
FT STRAND 412..414
FT /evidence="ECO:0007829|PDB:4XCI"
FT TURN 415..417
FT /evidence="ECO:0007829|PDB:4XCI"
FT HELIX 418..434
FT /evidence="ECO:0007829|PDB:4XCI"
FT HELIX 437..449
FT /evidence="ECO:0007829|PDB:4XCI"
FT HELIX 451..460
FT /evidence="ECO:0007829|PDB:4XCI"
FT HELIX 464..476
FT /evidence="ECO:0007829|PDB:4XCI"
FT STRAND 483..485
FT /evidence="ECO:0007829|PDB:4XCI"
FT TURN 486..489
FT /evidence="ECO:0007829|PDB:4XCI"
FT STRAND 490..493
FT /evidence="ECO:0007829|PDB:4XCI"
FT TURN 495..499
FT /evidence="ECO:0007829|PDB:4XCI"
FT STRAND 501..503
FT /evidence="ECO:0007829|PDB:4XCI"
FT HELIX 504..523
FT /evidence="ECO:0007829|PDB:4XCI"
FT STRAND 524..529
FT /evidence="ECO:0007829|PDB:4XCI"
SQ SEQUENCE 559 AA; 59675 MW; 46E6778E3A81F34C CRC64;
MAAPVLLLKE GTSRTTGRDA LRNNILAAKT LAEMLRSSLG PKGLDKMLID SFGDVTITND
GATIVKDMEI QHPAAKLLVE AAKAQDAEVG DGTTSAVVLA GALLEKAESL LDQNIHPTII
IEGYKKAYNK ALELLPQLGT RIDIKDLNSS VARDTLRKIA FTTLASKFIA EGAELNKIID
MVIDAIVNVA EPLPNGGYNV SLDLIKIDKK KGGSIEDSVL VKGLVLDKEV VHPGMPRRVT
KAKIAVLDAA LEVEKPEISA KISITSPEQI KAFLDEESKY LKDMVDKLAS IGANVVICQK
GIDDIAQHFL AKKGILAVRR VKRSDIEKLE KALGARIISS IKDATPEDLG YAELVEERRV
GNDKMVFIEG AKNLKAVNIL LRGSNDMALD EAERSINDAL HALRNILLEP VILPGGGAIE
LELAMKLREY ARSVGGKEQL AIEAFADALE EIPLILAETA GLEAISSLMD LRARHAKGLS
NTGVDVIGGK IVDDVYALNI IEPIRVKSQV LKSATEAATA ILKIDDLIAA APLKSEKKGG
EGSKEESGGE GGSTPSLGD
