ID   THSB_SACSH              Reviewed;         552 AA.
AC   P28488;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Thermosome subunit beta;
DE   AltName: Full=Chaperonin subunit beta;
DE   AltName: Full=Ring complex subunit beta;
DE   AltName: Full=Thermophilic factor 55 beta;
DE            Short=TF55-beta;
DE   AltName: Full=Thermosome subunit 2;
GN   Name=thsB; Synonyms=tf55;
OS   Saccharolobus shibatae (Sulfolobus shibatae).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=2286;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12;
RX   PubMed=1836250; DOI=10.1038/354490a0;
RA   Trent J.D., Nimmesgern E., Wall J.S., Hartl F.U., Horwich A.L.;
RT   "A molecular chaperone from a thermophilic archaebacterium is related to
RT   the eukaryotic protein T-complex polypeptide-1.";
RL   Nature 354:490-493(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.
RC   STRAIN=ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12;
RA   Osipiuk J., Trent J.D.;
RL   Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12;
RX   PubMed=7473746; DOI=10.1006/jmbi.1995.0585;
RA   Kagawa H.K., Osipiuk J., Maltsev N., Overbeek R., Quaite-Randall E.,
RA   Joachimiak A., Trent J.D.;
RT   "The 60 kDa heat shock proteins in the hyperthermophilic archaeon
RT   Sulfolobus shibatae.";
RL   J. Mol. Biol. 253:712-725(1995).
CC   -!- FUNCTION: Molecular chaperone; binds unfolded polypeptides in vitro,
CC       stimulates protein folding and has ATPase activity.
CC   -!- SUBUNIT: Forms a Heterooligomeric complex of two stacked nine-membered
CC       rings; one of alpha and the other of beta subunits.
CC   -!- INDUCTION: By heat shock.
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; X63834; CAA45326.1; -; Genomic_DNA.
DR   EMBL; L36863; AAA72454.1; -; Genomic_DNA.
DR   PIR; S19647; S19647.
DR   AlphaFoldDB; P28488; -.
DR   SMR; P28488; -.
DR   PRIDE; P28488; -.
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; Direct protein sequencing; Nucleotide-binding;
KW   Stress response.
FT   CHAIN           1..552
FT                   /note="Thermosome subunit beta"
FT                   /id="PRO_0000128405"
FT   REGION          531..552
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        537..552
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   552 AA;  59683 MW;  EBB6812FB67E3DCF CRC64;
     MATATVATTP EGIPVIILKE GSSRTYGKEA LRANIAAVKA IEEALKSTYG PRGMDKMFVD
     SLGDITITND GATILDKMDL QHPTGKLLVQ IAKGQDEETA DGTKTAVILA GELAKKAEDL
     LYKEIHPTII VSGYKKAEEI ALKTIQDIAQ PVSINDTDVL RKVALTSLGS KAVAGAREYL
     ADLVVKAVAQ VAELRGDKWY VDLDNVQIVK KHGGSINDTQ 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 AIKAATEAVT LVLRIDDIVA AGKKGGSEPG
     GKKEKEEKSS ED