THS_METKA
ID THS_METKA Reviewed; 545 AA.
AC P50016; Q49607;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Thermosome subunit;
DE AltName: Full=Chaperonin-like complex;
DE Short=CLIC;
GN Name=ths; OrderedLocusNames=MK1006;
OS Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC Methanopyrus.
OX NCBI_TaxID=190192;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX PubMed=8635576; DOI=10.1016/0014-5793(95)01493-4;
RA Andrae S., Frey G., Nitsch M., Baumeister W., Stetter K.O.;
RT "Purification and structural characterization of the thermosome from the
RT hyperthermophilic archaeum Methanopyrus kandleri.";
RL FEBS Lett. 379:127-131(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX PubMed=11930014; DOI=10.1073/pnas.032671499;
RA Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA Koonin E.V., Kozyavkin S.A.;
RT "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT monophyly of archaeal methanogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
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; Z50745; CAA90621.1; -; Genomic_DNA.
DR EMBL; Z49052; CAA88843.1; -; Genomic_DNA.
DR EMBL; AE009439; AAM02219.1; -; Genomic_DNA.
DR PIR; S54118; S54118.
DR PIR; S68687; S68687.
DR AlphaFoldDB; P50016; -.
DR SMR; P50016; -.
DR STRING; 190192.MK1006; -.
DR EnsemblBacteria; AAM02219; AAM02219; MK1006.
DR KEGG; mka:MK1006; -.
DR PATRIC; fig|190192.8.peg.1055; -.
DR HOGENOM; CLU_008891_7_3_2; -.
DR OMA; HPAANMI; -.
DR Proteomes; UP000001826; 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"
FT /id="PRO_0000128391"
SQ SEQUENCE 545 AA; 59474 MW; 775A89D3312AAF17 CRC64;
MAMLAGDGRQ VLILPEGYQR FVGRDAQRMN IMAARVVAET VRTTLGPMGM DKMLVDEMGD
VVVTNDGVTI LEEMDIEHPA AKMVVEVAKT QEDEVGDGTT TAVVLAGELL HKAEDLLQQD
IHPTVIARGY RMAVEKAEEI LEEIAEEIDP DDEETLKKIA KTAMTGKGVE KARDYLAELV
VKAVKQVAEE EDGEIVIDTD HIKLEKKEGG GLEDTELVKG MVIDKERVHP GMPRRVENAK
IALLNCPIEV KETETDAEIR ITDPEQLQAF IEEEERMLSE MVDKIAETGA NVVFCQKGID
DLAQHYLAKK GILAVRRVKK SDMQKLARAT GARIVTNIDD LSEEDLGEAE VVEEKKVAGD
KMIFVEGCKD PKAVTILIRG GTEHVVDEAE RAIEDAIGVV AAALEDGKVV AGGGAPEVEV
ARQLRDFADG VEGREQLAVE AFADALEIIP RTLAENSGLD PIDVLVQLRA KHEDGQVTAG
IDVYDGDVKD MLEEGVVEPL RVKTQALASA TEAAEMILRI DDVIAARELS KEEEEEEEEG
GSSEF