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 27-MAR-2024, entry version 152. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.gene:9572500; -. DR PaxDb; 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 InParanoid; P48425; -. DR OrthoDB; 9362at2157; -. 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; 3.50.7.10; GroEL; 1. DR Gene3D; 1.10.560.10; GroEL-like equatorial domain; 1. DR Gene3D; 3.30.260.10; TCP-1-like chaperonin intermediate domain; 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 NCBIfam; NF041082; thermosome_alpha; 1. DR NCBIfam; TIGR02339; thermosome_arch; 1. DR NCBIfam; NF041083; thermosome_beta; 1. DR PANTHER; PTHR11353; CHAPERONIN; 1. DR PANTHER; PTHR11353:SF94; T-COMPLEX PROTEIN 1 SUBUNIT EPSILON; 1. DR Pfam; PF00118; Cpn60_TCP1; 1. DR PRINTS; PR00304; TCOMPLEXTCP1. DR SUPFAM; SSF52029; GroEL apical domain-like; 1. DR SUPFAM; SSF48592; GroEL equatorial domain-like; 1. DR SUPFAM; SSF54849; GroEL-intermediate domain like; 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 //