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EFTS_THET8
ID   EFTS_THET8              Reviewed;         196 AA.
AC   P43895; Q5SJZ2;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 141.
DE   RecName: Full=Elongation factor Ts;
DE            Short=EF-Ts;
GN   Name=tsf; OrderedLocusNames=TTHA0860;
OS   Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=300852;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8617268; DOI=10.1111/j.1432-1033.1996.00222.x;
RA   Blank J., Nock S., Kreutzer R., Sprinzl M.;
RT   "Elongation factor Ts from Thermus thermophilus -- overproduction in
RT   Escherichia coli, quaternary structure and interaction with elongation
RT   factor Tu.";
RL   Eur. J. Biochem. 236:222-227(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27634 / DSM 579 / HB8;
RA   Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA   Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT   "Complete genome sequence of Thermus thermophilus HB8.";
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF COMPLEX WITH EF-TU.
RX   PubMed=9253415; DOI=10.1038/nsb0897-650;
RA   Wang Y., Jiang Y., Meyering-Voss M., Sprinzl M., Sigler P.B.;
RT   "Crystal structure of the EF-Tu.EF-Ts complex from Thermus thermophilus.";
RL   Nat. Struct. Biol. 4:650-656(1997).
CC   -!- FUNCTION: Associates with the EF-Tu.GDP complex and induces the
CC       exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-
CC       Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.
CC   -!- SUBUNIT: Heterotetramer composed of two EF-Ts.EF-Tu dimer complexes.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the EF-Ts family. {ECO:0000305}.
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DR   EMBL; X83598; CAA58578.1; -; Genomic_DNA.
DR   EMBL; AP008226; BAD70683.1; -; Genomic_DNA.
DR   RefSeq; WP_011228249.1; NC_006461.1.
DR   RefSeq; YP_144126.1; NC_006461.1.
DR   PDB; 1AIP; X-ray; 3.00 A; C/D/G/H=1-196.
DR   PDB; 1TFE; X-ray; 1.70 A; A=55-196.
DR   PDBsum; 1AIP; -.
DR   PDBsum; 1TFE; -.
DR   AlphaFoldDB; P43895; -.
DR   SMR; P43895; -.
DR   DIP; DIP-6078N; -.
DR   IntAct; P43895; 1.
DR   STRING; 300852.55772242; -.
DR   EnsemblBacteria; BAD70683; BAD70683; BAD70683.
DR   GeneID; 3170120; -.
DR   KEGG; ttj:TTHA0860; -.
DR   PATRIC; fig|300852.9.peg.854; -.
DR   eggNOG; COG0264; Bacteria.
DR   HOGENOM; CLU_047155_1_1_0; -.
DR   OMA; DAGMMDC; -.
DR   PhylomeDB; P43895; -.
DR   EvolutionaryTrace; P43895; -.
DR   Proteomes; UP000000532; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.479.20; -; 1.
DR   HAMAP; MF_00050; EF_Ts; 1.
DR   InterPro; IPR036402; EF-Ts_dimer_sf.
DR   InterPro; IPR001816; Transl_elong_EFTs/EF1B.
DR   InterPro; IPR014039; Transl_elong_EFTs/EF1B_dimer.
DR   InterPro; IPR018101; Transl_elong_Ts_CS.
DR   InterPro; IPR009060; UBA-like_sf.
DR   PANTHER; PTHR11741; PTHR11741; 1.
DR   Pfam; PF00889; EF_TS; 1.
DR   SUPFAM; SSF46934; SSF46934; 1.
DR   SUPFAM; SSF54713; SSF54713; 1.
DR   TIGRFAMs; TIGR00116; tsf; 1.
DR   PROSITE; PS01126; EF_TS_1; 1.
DR   PROSITE; PS01127; EF_TS_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Elongation factor; Protein biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..196
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_0000161222"
FT   REGION          80..83
FT                   /note="Involved in Mg(2+) ion dislocation from EF-Tu"
FT                   /evidence="ECO:0000250"
FT   HELIX           3..14
FT                   /evidence="ECO:0007829|PDB:1AIP"
FT   HELIX           18..27
FT                   /evidence="ECO:0007829|PDB:1AIP"
FT   TURN            28..30
FT                   /evidence="ECO:0007829|PDB:1AIP"
FT   HELIX           32..50
FT                   /evidence="ECO:0007829|PDB:1AIP"
FT   STRAND          57..64
FT                   /evidence="ECO:0007829|PDB:1TFE"
FT   STRAND          68..79
FT                   /evidence="ECO:0007829|PDB:1TFE"
FT   HELIX           81..85
FT                   /evidence="ECO:0007829|PDB:1TFE"
FT   HELIX           87..103
FT                   /evidence="ECO:0007829|PDB:1TFE"
FT   STRAND          106..109
FT                   /evidence="ECO:0007829|PDB:1TFE"
FT   HELIX           110..112
FT                   /evidence="ECO:0007829|PDB:1TFE"
FT   HELIX           115..130
FT                   /evidence="ECO:0007829|PDB:1TFE"
FT   TURN            131..133
FT                   /evidence="ECO:0007829|PDB:1TFE"
FT   HELIX           136..154
FT                   /evidence="ECO:0007829|PDB:1TFE"
FT   HELIX           156..158
FT                   /evidence="ECO:0007829|PDB:1TFE"
FT   STRAND          159..161
FT                   /evidence="ECO:0007829|PDB:1TFE"
FT   STRAND          164..168
FT                   /evidence="ECO:0007829|PDB:1TFE"
FT   HELIX           169..180
FT                   /evidence="ECO:0007829|PDB:1TFE"
FT   STRAND          185..193
FT                   /evidence="ECO:0007829|PDB:1TFE"
SQ   SEQUENCE   196 AA;  22413 MW;  36A771F686BBB0DD CRC64;
     MSQMELIKKL REATGAGMMD VKRALEDAGW DEEKAVQLLR ERGAMKAAKK ADREAREGII
     GHYIHHNQRV GVLVELNCET DFVARNELFQ NLAKDLAMHI AMMNPRYVSA EEIPAEELEK
     ERQIYIQAAL NEGKPQQIAE KIAEGRLKKY LEEVVLLEQP FVKDDKVKVK ELIQQAIAKI
     GENIVVRRFC RFELGA
 
 
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