ID   THS_METTL               Reviewed;         544 AA.
AC   O93624;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Thermosome subunit;
DE   AltName: Full=Chaperonin subunit;
GN   Name=ths;
OS   Methanothermococcus thermolithotrophicus (Methanococcus
OS   thermolithotrophicus).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanothermococcus.
OX   NCBI_TaxID=2186;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC   STRAIN=ATCC 35097 / DSM 2095 / JCM 10549 / OCM 138 / SN-1;
RX   PubMed=9774467; DOI=10.1074/jbc.273.43.28399;
RA   Furutani M., Iida T., Yoshida T., Maruyama T.;
RT   "Group II chaperonin in a thermophilic methanogen, Methanococcus
RT   thermolithotrophicus. Chaperone activity and filament-forming ability.";
RL   J. Biol. Chem. 273:28399-28407(1998).
CC   -!- FUNCTION: Molecular chaperone; binds unfolded polypeptides in vitro,
CC       and has a weak ATPase activity.
CC   -!- SUBUNIT: Forms an oligomeric complex of eight-membered rings.
CC   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR   EMBL; AB015435; BAA33889.1; -; Genomic_DNA.
DR   PIR; T43845; T43845.
DR   AlphaFoldDB; O93624; -.
DR   SMR; O93624; -.
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; Nucleotide-binding.
FT   CHAIN           1..544
FT                   /note="Thermosome subunit"
FT                   /id="PRO_0000128392"
SQ   SEQUENCE   544 AA;  58638 MW;  4128761D958CFCE6 CRC64;
     MAANQPVVVL PENVKRFMGR DAQRMNILAG RIIGETVRST LGPKGMDKML VDDLGDIVVT
     NDGVTILKEM SVEHPAAKML IEVAKTQEKE VGDGTTTAVV IAGELLRKAE ELLDQNVHPT
     IVIKGYQLAV QKAQEVLKEI AMDVKADDKE ILHKIAMTSI TGKGAEKAKE KLGEMIVEAV
     TAVVDESGKV DKDLIKIEKK EGASVDETEL INGVLIDKER VSPQMPKKIE NAKIALLNCP
     IEVKETETDA EIRITDPTKL MEFIEQEEKM LKDMVDTIKA SGANVLFCQK GIDDLAQHYL
     AKEGILAVRR VKKSDMEKLS KATGANVVTN IKDLKAEDLG EAGIVEERKI AGDAMIFVEE
     CKHPKAVTML IRGTTEHVIE EVARAVDDAI GVVACTIEDG KIVAGGGAAE IELAMKLRDY
     AEGVSGREQL AVRAFADALE VVPRTLAENA GLDAIEMLVK LRAKHAEGNN AYYGLNVFTG
     DVENMTENGV VEPLRVKTQA IQSATEATEM LLRIDDVIAA EKLSGGSGGD MGDMGGMGGM
     GGMM