ID   THSB_DESMO              Reviewed;         502 AA.
AC   Q9V2T3;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Thermosome subunit beta;
DE   AltName: Full=Chaperonin subunit beta;
DE   AltName: Full=Thermosome subunit 2;
DE   Flags: Fragment;
GN   Name=thsB;
OS   Desulfurococcus mucosus (Desulfurococcus mobilis).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Desulfurococcus.
OX   NCBI_TaxID=2275;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR   EMBL; AF149925; AAF03366.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9V2T3; -.
DR   SMR; Q9V2T3; -.
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.
FT   CHAIN           <1..>502
FT                   /note="Thermosome subunit beta"
FT                   /id="PRO_0000128383"
FT   NON_TER         1
FT   NON_TER         502
SQ   SEQUENCE   502 AA;  54964 MW;  E3004454E9352925 CRC64;
     QRTTGRDALR TNILAARAIS EMIKTTYGPK GMDKMLVDAL GDVTITNDGA TILDKAEIQH
     PAAKMLVQVA KSQDSEVGDG TKRAVILAGE LLKYAEELLD KNIHPTVIIS GYRMAMEEAL
     KILDQMAEPI DLNNEELLRK VARTSLTSKA VHDAREFFAD IAVKAVKQVV EKRGDKNYVD
     LDNIQIIKKY GGALLDSMLV YGIVLDKEVV HPGMPRRVEN AKIVLLDAPL EIEKPEIDAE
     IRINDPEQLE KFLQQEEEIL MKMVDKIASV GANVVVCQKG IDEVAQHFLA KKGILAVRRV
     KRSDLEKLER ATGGRIVSNI EDLTPEDLGY AALVEERKVG EDKMVFIEGC KNPRSVSIVI
     RGGLERLVDE AERSIRDALS AVADALRDGK VIPGGGAAEI ELAKHIRRLA TRVGGKEQLA
     IEAFAKALEG LAVTLVENAG LDPIDMVMKL RAAHEREDGK YLSIDLATGD LVNMREKGVI
     EPVSILANAI KAGTEAATII MR