THSB_THEAC
ID THSB_THEAC Reviewed; 543 AA.
AC P48425;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Thermosome subunit beta;
DE AltName: Full=Chaperonin subunit beta;
DE AltName: Full=Thermosome subunit 2;
GN Name=thsB; OrderedLocusNames=Ta1276;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 188-195.
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=7794526; DOI=10.1515/bchm3.1995.376.2.119;
RA Waldmann T., Lupas A.N., Kellermann J., Peters J., Baumeister W.;
RT "Primary structure of the thermosome from Thermoplasma acidophilum.";
RL Biol. Chem. Hoppe-Seyler 376:119-126(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
RN [3]
RP PROTEIN SEQUENCE OF 80-113 AND 421-445.
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=7867646; DOI=10.1111/j.1432-1033.1995.tb20210.x;
RA Waldmann T., Nimmesgern E., Nitsch M., Peters J., Pfeifer G., Mueller S.,
RA Kellermann J., Engel A., Hartl F.-U., Baumeister W.;
RT "The thermosome of Thermoplasma acidophilum and its relationship to the
RT eukaryotic chaperonin TRiC.";
RL Eur. J. Biochem. 227:848-856(1995).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
RX PubMed=9546398; DOI=10.1016/s0092-8674(00)81152-6;
RA Ditzel L., Loewe J., Stock D., Stetter K.-O., Huber H., Huber R.,
RA Steinbacher S.;
RT "Crystal structure of the thermosome, the archaeal chaperonin and homolog
RT of CCT.";
RL Cell 93:125-138(1998).
CC -!- FUNCTION: Molecular chaperone; binds unfolded polypeptides in vitro,
CC and has a weak ATPase activity.
CC -!- SUBUNIT: Forms a Heterooligomeric complex of two stacked eight-membered
CC rings.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR EMBL; Z46650; CAA86611.1; -; Genomic_DNA.
DR EMBL; AL445067; CAC12400.1; -; Genomic_DNA.
DR PIR; S53817; S53817.
DR RefSeq; WP_010901684.1; NC_002578.1.
DR PDB; 1A6D; X-ray; 2.60 A; B=1-543.
DR PDB; 1A6E; X-ray; 3.20 A; B=1-543.
DR PDB; 1E0R; X-ray; 2.80 A; B=214-367.
DR PDBsum; 1A6D; -.
DR PDBsum; 1A6E; -.
DR PDBsum; 1E0R; -.
DR AlphaFoldDB; P48425; -.
DR BMRB; P48425; -.
DR SMR; P48425; -.
DR MINT; P48425; -.
DR STRING; 273075.Ta1276; -.
DR EnsemblBacteria; CAC12400; CAC12400; CAC12400.
DR GeneID; 1456762; -.
DR KEGG; tac:Ta1276; -.
DR eggNOG; arCOG01257; Archaea.
DR HOGENOM; CLU_008891_7_3_2; -.
DR OMA; KNYKNYG; -.
DR OrthoDB; 11742at2157; -.
DR BRENDA; 3.6.4.B10; 6324.
DR BRENDA; 5.6.1.7; 6324.
DR EvolutionaryTrace; P48425; -.
DR Proteomes; UP000001024; 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 3D-structure; ATP-binding; Chaperone; Direct protein sequencing;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..543
FT /note="Thermosome subunit beta"
FT /id="PRO_0000128410"
FT REGION 522..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 21..38
FT /evidence="ECO:0007829|PDB:1A6D"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:1A6D"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:1A6D"
FT HELIX 63..69
FT /evidence="ECO:0007829|PDB:1A6D"
FT HELIX 75..84
FT /evidence="ECO:0007829|PDB:1A6D"
FT HELIX 94..114
FT /evidence="ECO:0007829|PDB:1A6D"
FT HELIX 119..140
FT /evidence="ECO:0007829|PDB:1A6D"
FT HELIX 148..160
FT /evidence="ECO:0007829|PDB:1A6D"
FT HELIX 164..168
FT /evidence="ECO:0007829|PDB:1A6D"
FT HELIX 169..183
FT /evidence="ECO:0007829|PDB:1A6D"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:1A6D"
FT STRAND 188..193
FT /evidence="ECO:0007829|PDB:1A6D"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:1A6D"
FT STRAND 198..206
FT /evidence="ECO:0007829|PDB:1A6D"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:1A6D"
FT STRAND 212..220
FT /evidence="ECO:0007829|PDB:1A6D"
FT STRAND 230..242
FT /evidence="ECO:0007829|PDB:1A6D"
FT STRAND 250..255
FT /evidence="ECO:0007829|PDB:1A6D"
FT HELIX 262..283
FT /evidence="ECO:0007829|PDB:1A6D"
FT STRAND 288..293
FT /evidence="ECO:0007829|PDB:1A6D"
FT HELIX 297..305
FT /evidence="ECO:0007829|PDB:1A6D"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:1A6D"
FT HELIX 316..326
FT /evidence="ECO:0007829|PDB:1A6D"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:1A6D"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:1A6D"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:1A6D"
FT STRAND 343..353
FT /evidence="ECO:0007829|PDB:1A6D"
FT STRAND 356..368
FT /evidence="ECO:0007829|PDB:1A6D"
FT STRAND 370..378
FT /evidence="ECO:0007829|PDB:1A6D"
FT HELIX 379..402
FT /evidence="ECO:0007829|PDB:1A6D"
FT STRAND 404..407
FT /evidence="ECO:0007829|PDB:1A6D"
FT TURN 408..410
FT /evidence="ECO:0007829|PDB:1A6D"
FT HELIX 411..426
FT /evidence="ECO:0007829|PDB:1A6D"
FT HELIX 431..442
FT /evidence="ECO:0007829|PDB:1A6D"
FT HELIX 444..453
FT /evidence="ECO:0007829|PDB:1A6D"
FT HELIX 457..469
FT /evidence="ECO:0007829|PDB:1A6D"
FT STRAND 475..478
FT /evidence="ECO:0007829|PDB:1A6D"
FT TURN 479..482
FT /evidence="ECO:0007829|PDB:1A6D"
FT STRAND 483..486
FT /evidence="ECO:0007829|PDB:1A6D"
FT TURN 487..491
FT /evidence="ECO:0007829|PDB:1A6D"
FT STRAND 493..495
FT /evidence="ECO:0007829|PDB:1A6D"
FT HELIX 496..515
FT /evidence="ECO:0007829|PDB:1A6D"
FT STRAND 516..520
FT /evidence="ECO:0007829|PDB:1A6D"
SQ SEQUENCE 543 AA; 58480 MW; F9CDAEE63E8B84E6 CRC64;
MIAGQPIFIL KEGTKRESGK DAMKENIEAA IAISNSVRSS LGPRGMDKML VDSLGDIVIT
NDGVTILKEM DVEHPAAKMM VEVSKTQDSF VGDGTTTAVI IAGGLLQQAQ GLINQNVHPT
VISEGYRMAS EEAKRVIDEI STKIGADEKA LLLKMAQTSL NSKSASVAKD KLAEISYEAV
KSVAELRDGK YYVDFDNIQV VKKQGGAIDD TQLINGIIVD KEKVHPGMPD VVKDAKIALL
DAPLEIKKPE FDTNLRIEDP SMIQKFLAQE ENMLREMVDK IKSVGANVVI TQKGIDDMAQ
HYLSRAGIYA VRRVKKSDMD KLAKATGASI VSTIDEISSS DLGTAERVEQ VKVGEDYMTF
VTGCKNPKAV SILVRGETEH VVDEMERSIT DSLHVVASAL EDGAYAAGGG ATAAEIAFRL
RSYAQKIGGR QQLAIEKFAD AIEEIPRALA ENAGLDPIDI LLKLRAEHAK GNKTYGINVF
TGEIEDMVKN GVIEPIRVGK QAIESATEAA IMILRIDDVI ATKSSSSSSN PPKSGSSSES
SED
