THS_METJA
ID THS_METJA Reviewed; 542 AA.
AC Q58405;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Thermosome subunit;
DE AltName: Full=Chaperonin subunit;
GN Name=ths; OrderedLocusNames=MJ0999;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
CC -!- FUNCTION: Molecular chaperone; binds unfolded polypeptides in vitro,
CC and has a weak ATPase activity. {ECO:0000250}.
CC -!- SUBUNIT: Forms an oligomeric complex of eight-membered rings.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR EMBL; L77117; AAB99002.1; -; Genomic_DNA.
DR PIR; F64424; F64424.
DR RefSeq; WP_010870512.1; NC_000909.1.
DR AlphaFoldDB; Q58405; -.
DR SMR; Q58405; -.
DR STRING; 243232.MJ_0999; -.
DR EnsemblBacteria; AAB99002; AAB99002; MJ_0999.
DR GeneID; 1451896; -.
DR KEGG; mja:MJ_0999; -.
DR eggNOG; arCOG01257; Archaea.
DR HOGENOM; CLU_008891_7_3_2; -.
DR InParanoid; Q58405; -.
DR OMA; HPAANMI; -.
DR OrthoDB; 11742at2157; -.
DR PhylomeDB; Q58405; -.
DR Proteomes; UP000000805; 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; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
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..542
FT /note="Thermosome subunit"
FT /id="PRO_0000128390"
SQ SEQUENCE 542 AA; 58772 MW; D505F08531D4668D CRC64;
MAMAGAPIVV LPQNVKRYVG RDAQRMNILA GRIIAETVRT TLGPKGMDKM LVDELGDIVV
TNDGVTILKE MSVEHPAAKM LIEVAKTQEK EVGDGTTTAV VIAGELLRKA EELLDQNIHP
SVIINGYEMA RNKAVEELKS IAKEVKPEDT EMLKKIAMTS ITGKGAEKAR EQLAEIVVEA
VRAVVDEETG KVDKDLIKVE KKEGAPIEET KLIRGVVIDK ERVNPQMPKK VENAKIALLN
CPIEVKETET DAEIRITDPA KLMEFIEQEE KMIKDMVEKI AATGANVVFC QKGIDDLAQH
YLAKKGILAV RRVKKSDMEK LAKATGARIV TKIDDLTPED LGEAGLVEER KVAGDAMIFV
EQCKHPKAVT ILARGSTEHV VEEVARAIDD AIGVVKCALE EGKIVAGGGA TEIELAKRLR
KFAESVAGRE QLAVKAFADA LEVIPRTLAE NSGLDPIDML VKLRAAHEKE GGEVYGLDVF
EGEVVDMLEK GVVEPLKVKT QAIDSATEAS VMLLRIDDVI AAEKVKGDEK GGEGGDMGGD
EF