ID   THSB_AERPE              Reviewed;         548 AA.
AC   Q9YA66;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2001, sequence version 2.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Thermosome subunit beta;
DE   AltName: Full=Chaperonin subunit beta;
DE   AltName: Full=Thermosome subunit 2;
GN   Name=thsB; OrderedLocusNames=APE_2072.1;
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS   K1).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA   Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA   Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT   Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(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; BA000002; BAA81083.2; -; Genomic_DNA.
DR   PIR; C72512; C72512.
DR   AlphaFoldDB; Q9YA66; -.
DR   SMR; Q9YA66; -.
DR   STRING; 272557.APE_2072.1; -.
DR   EnsemblBacteria; BAA81083; BAA81083; APE_2072.1.
DR   KEGG; ape:APE_2072.1; -.
DR   PATRIC; fig|272557.25.peg.1379; -.
DR   eggNOG; arCOG01257; Archaea.
DR   OMA; HPAANMI; -.
DR   BRENDA; 3.6.4.B10; 171.
DR   Proteomes; UP000002518; 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..548
FT                   /note="Thermosome subunit beta"
FT                   /id="PRO_0000128380"
SQ   SEQUENCE   548 AA;  60430 MW;  4AC10DD3F7B035FE CRC64;
     MAIQQQPMTE PVGIPVIILK EGTQRSYGRE ALRANIMAVR AIAQILKTTY GPKGMDKMLV
     DSLGDITITN NGATILDKMD VAHPAAKMLV QISKGQEDEA GDGTKTTVIF AGELLKEAEK
     LLDINIHPTI IVEGYKEALR KASEVIESIA EPVSYDDVEK LKLIAKTSLN SKAVAEARDY
     FAELAVEAVR TVAERRGDRW YVDLNNIQIV KKHGGSLRDT RLVRGIVLDK EVVHPDMPRR
     VENARIALLD TPLEIEKPEI DLEISITSPE QIKALYEKQE RILQEKIEKI AATGANVVIT
     QKGIDDVAQH FLAKKGILAV RRVKRSDIEK IARATGARIV TDIEDLRPED LGYAELVEER
     KVGEDKMVFI EGAKNPKSVT ILLRGGFERL VDEAERSLHD ALSVVADAIM DGKIVAGGGA
     VEAEVAKVLY EYASKLPGKT QLAVEAFARA VEALPQALAH NAGHDPIEVL VKLRSAHEKP
     ENKWYGVDLD TGEIVDMWSR GVLEPMRVKL NALKAATEVA SLILRIDDVI AARKEEEEKE
     EKRGGEEE