THSB_SACS2
ID THSB_SACS2 Reviewed; 554 AA.
AC Q9V2T8;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Thermosome subunit beta;
DE AltName: Full=Chaperonin subunit beta;
DE AltName: Full=Thermophilic factor 55 beta;
DE Short=TF55-beta;
DE AltName: Full=Thermosome subunit 2;
GN Name=thsB; OrderedLocusNames=SSO0282;
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 [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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 103-524.
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).
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 Q9V2T8; Q9V2S9: thsA; NbExp=7; IntAct=EBI-16195251, EBI-16195227;
CC Q9V2T8; Q9V2T8: thsB; NbExp=4; IntAct=EBI-16195251, EBI-16195251;
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK40620.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE006641; AAK40620.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF149920; AAF03361.1; -; Genomic_DNA.
DR PIR; E90170; E90170.
DR RefSeq; WP_009990564.1; NC_002754.1.
DR PDB; 4XCD; X-ray; 3.79 A; A/B/C/D/E/F=1-554.
DR PDB; 4XCG; X-ray; 3.74 A; B=1-554.
DR PDB; 4XCI; X-ray; 3.00 A; B=1-554.
DR PDB; 6XHI; EM; 4.19 A; A=1-554.
DR PDB; 6XHJ; EM; 3.62 A; A=1-554.
DR PDBsum; 4XCD; -.
DR PDBsum; 4XCG; -.
DR PDBsum; 4XCI; -.
DR PDBsum; 6XHI; -.
DR PDBsum; 6XHJ; -.
DR AlphaFoldDB; Q9V2T8; -.
DR SMR; Q9V2T8; -.
DR DIP; DIP-61907N; -.
DR IntAct; Q9V2T8; 1.
DR STRING; 273057.SSO0282; -.
DR EnsemblBacteria; AAK40620; AAK40620; SSO0282.
DR GeneID; 44129253; -.
DR KEGG; sso:SSO0282; -.
DR PATRIC; fig|273057.12.peg.276; -.
DR eggNOG; arCOG01257; Archaea.
DR HOGENOM; CLU_008891_7_3_2; -.
DR InParanoid; Q9V2T8; -.
DR OMA; HPAANMI; -.
DR PhylomeDB; Q9V2T8; -.
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:0042802; F:identical protein binding; IPI:IntAct.
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..554
FT /note="Thermosome subunit beta"
FT /id="PRO_0000128402"
FT REGION 532..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..554
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 298
FT /note="I -> M (in Ref. 2)"
FT /evidence="ECO:0000305"
FT HELIX 29..46
FT /evidence="ECO:0007829|PDB:4XCI"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:4XCI"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:4XCI"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:4XCI"
FT HELIX 71..77
FT /evidence="ECO:0007829|PDB:4XCI"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:4XCI"
FT HELIX 86..92
FT /evidence="ECO:0007829|PDB:4XCI"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:4XCI"
FT HELIX 102..121
FT /evidence="ECO:0007829|PDB:4XCI"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:4XCI"
FT HELIX 127..148
FT /evidence="ECO:0007829|PDB:4XCI"
FT HELIX 157..167
FT /evidence="ECO:0007829|PDB:4XCI"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:4XCI"
FT HELIX 177..191
FT /evidence="ECO:0007829|PDB:4XCI"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:4XCI"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:4XCI"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:4XCI"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:4XCI"
FT STRAND 219..227
FT /evidence="ECO:0007829|PDB:4XCI"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:4XCI"
FT HELIX 281..289
FT /evidence="ECO:0007829|PDB:4XCI"
FT HELIX 305..313
FT /evidence="ECO:0007829|PDB:4XCI"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:4XCI"
FT HELIX 324..334
FT /evidence="ECO:0007829|PDB:4XCI"
FT STRAND 355..361
FT /evidence="ECO:0007829|PDB:4XCI"
FT STRAND 364..370
FT /evidence="ECO:0007829|PDB:4XCI"
FT STRAND 378..383
FT /evidence="ECO:0007829|PDB:4XCI"
FT HELIX 387..410
FT /evidence="ECO:0007829|PDB:4XCI"
FT STRAND 412..415
FT /evidence="ECO:0007829|PDB:4XCI"
FT TURN 416..418
FT /evidence="ECO:0007829|PDB:4XCI"
FT HELIX 419..431
FT /evidence="ECO:0007829|PDB:4XCI"
FT HELIX 432..434
FT /evidence="ECO:0007829|PDB:4XCI"
FT HELIX 437..460
FT /evidence="ECO:0007829|PDB:4XCI"
FT HELIX 465..475
FT /evidence="ECO:0007829|PDB:4XCI"
FT HELIX 479..481
FT /evidence="ECO:0007829|PDB:4XCI"
FT STRAND 484..486
FT /evidence="ECO:0007829|PDB:4XCI"
FT TURN 488..490
FT /evidence="ECO:0007829|PDB:4XCI"
FT STRAND 492..495
FT /evidence="ECO:0007829|PDB:4XCI"
FT TURN 496..500
FT /evidence="ECO:0007829|PDB:4XCI"
FT STRAND 502..504
FT /evidence="ECO:0007829|PDB:4XCI"
FT HELIX 505..524
FT /evidence="ECO:0007829|PDB:4XCI"
SQ SEQUENCE 554 AA; 59952 MW; 927BF96B78A59547 CRC64;
MATATVATTP EGIPVIILKE GSSRTYGKEA LRANIAAVKA IEEALKSTYG PRGMDKMLVD
SLGDITITND GATILDKMDL QHPTGKLLVQ IAKGQDEETA DGTKTAVILA GELAKKAEDL
LYKEIHPTII VSGYKKAEEI ALKTIQEIAQ PVTINDTDVL RKVALTSLGS KAVAGAREYL
ADLVVKAVAQ VAELRGDKWY VDLDNVQIVK KHGGSVNDTQ LVYGIVVDKE VVHPGMPKRI
ENAKIALLDA SLEVEKPELD AEIRINDPTQ MHKFLEEEEN ILKEKVDKIA ATGANVVICQ
KGIDEVAQHY LAKKGILAVR RAKKSDLEKL ARATGGRVIS NIDELTSQDL GYAALVEERK
VGEDKMVFVE GAKNPKSVSI LIRGGLERVV DETERALRDA LGTVADVIRD GRAVAGGGAV
EIEIAKRLRK YAPQVGGKEQ LAIEAYANAI EGLIMILAEN AGLDPIDKLM QLRSLHENET
NKWYGLNLFT GNPEDMWKLG VIEPALVKMN AVKAATEAVT LVLRIDDIVA AGKKSGSEPS
GKKEKDKEEK SSED