ID   THSB_ARCFU              Reviewed;         545 AA.
AC   O28821;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Thermosome subunit beta;
DE   AltName: Full=Chaperonin subunit beta;
DE   AltName: Full=Thermosome subunit 2;
GN   Name=thsB; OrderedLocusNames=AF_1451;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS   100126 / VC-16).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA   Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA   Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA   Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA   Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA   Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA   Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA   Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA   Smith H.O., Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT   archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RA   Emmerhoff O.J., Birkeland N.-K.;
RL   Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR   EMBL; AE000782; AAB89798.1; -; Genomic_DNA.
DR   PIR; B69431; B69431.
DR   RefSeq; WP_010878948.1; NC_000917.1.
DR   AlphaFoldDB; O28821; -.
DR   SMR; O28821; -.
DR   STRING; 224325.AF_1451; -.
DR   EnsemblBacteria; AAB89798; AAB89798; AF_1451.
DR   GeneID; 24795063; -.
DR   KEGG; afu:AF_1451; -.
DR   eggNOG; arCOG01257; Archaea.
DR   HOGENOM; CLU_008891_7_3_2; -.
DR   OMA; HPAANMI; -.
DR   OrthoDB; 11742at2157; -.
DR   PhylomeDB; O28821; -.
DR   Proteomes; UP000002199; 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   3: Inferred from homology;
KW   ATP-binding; Chaperone; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..545
FT                   /note="Thermosome subunit beta"
FT                   /id="PRO_0000128382"
SQ   SEQUENCE   545 AA;  58684 MW;  CA3DA663A4A842F2 CRC64;
     MATLQGQPVL ILREGTQRTV GRDAQRMNIM AARVIAEAVR STLGPKGMDK MLVDSLGDVV
     ITNDGVTILK EIDVEHPAAK MIIEVAKTQD NEVGDGTTTA VVLAGELLKR AEELLDQEIH
     PAIIANGYRY AAEKALEILN EIAIPISKDD DEILKKIATT AMTGKGAEVA IDKLAEIAVN
     AVKMIAEESN GQVEVNTDYI KIEKRQGGSI EETELVDGIV LDKEVVHPGM PKRVENAKIL
     LLDSALEVKE TEIDAKIRIT DPEKLQKFIE QEEAMLKEMV DKIVNAGANV VFCQKGIDDL
     AQYYLAKAGV LAVRRVKKSD MEKLAKATGA KVLTDLRDIS SEDLGEAALV EERKVGDEKM
     VFVTGCKNPK AVTILVRGGT EHVVEEIARG IEDAVRAVAC AVEDGKVVVG AGAPEIEVSL
     KLREWAPSLG GREQLAVEAF ATALEIIPRT LAENAGLDPI DVLVELKAAH EKGQKYAGVD
     VDTGKVVDMK ERGVFEPLRV KTQAIGSATE VAVMILRIDD IIAAKGLEKE KGGGGEGGMP
     EMPEF