ID   EFTS_THEYD              Reviewed;         199 AA.
AC   B5YGE0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Elongation factor Ts {ECO:0000255|HAMAP-Rule:MF_00050};
DE            Short=EF-Ts {ECO:0000255|HAMAP-Rule:MF_00050};
GN   Name=tsf {ECO:0000255|HAMAP-Rule:MF_00050}; OrderedLocusNames=THEYE_A1542;
OS   Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87).
OC   Bacteria; Nitrospirae; Thermodesulfovibrionia; Thermodesulfovibrionales;
OC   Thermodesulfovibrionaceae; Thermodesulfovibrio.
OX   NCBI_TaxID=289376;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51303 / DSM 11347 / YP87;
RA   Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT   "The complete genome sequence of Thermodesulfovibrio yellowstonii strain
RT   ATCC 51303 / DSM 11347 / YP87.";
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
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       {ECO:0000255|HAMAP-Rule:MF_00050}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00050}.
CC   -!- SIMILARITY: Belongs to the EF-Ts family. {ECO:0000255|HAMAP-
CC       Rule:MF_00050}.
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DR   EMBL; CP001147; ACI20484.1; -; Genomic_DNA.
DR   RefSeq; WP_012545220.1; NC_011296.1.
DR   RefSeq; YP_002249338.1; NC_011296.1.
DR   AlphaFoldDB; B5YGE0; -.
DR   SMR; B5YGE0; -.
DR   STRING; 289376.THEYE_A1542; -.
DR   PRIDE; B5YGE0; -.
DR   EnsemblBacteria; ACI20484; ACI20484; THEYE_A1542.
DR   KEGG; tye:THEYE_A1542; -.
DR   PATRIC; fig|289376.4.peg.1500; -.
DR   eggNOG; COG0264; Bacteria.
DR   HOGENOM; CLU_047155_1_1_0; -.
DR   InParanoid; B5YGE0; -.
DR   OMA; DAGMMDC; -.
DR   OrthoDB; 1405357at2; -.
DR   Proteomes; UP000000718; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR   GO; GO:0006414; P:translational elongation; IBA:GO_Central.
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   3: Inferred from homology;
KW   Cytoplasm; Elongation factor; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..199
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_1000189893"
FT   REGION          80..83
FT                   /note="Involved in Mg(2+) ion dislocation from EF-Tu"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00050"
SQ   SEQUENCE   199 AA;  22832 MW;  6934DD216A60BEBD CRC64;
     MAITAQMVKE LREKTGAGMM ECKKALETSG GDFNKAIDIL RQKGLATAQK KASREAKEGI
     ITSYIHMDKI GVMLELNCET DFVARNEEFR QLAKDIAMQI AASNPQYIQR EDIPQEVIEK
     EKEIYKSQIK GNKPPQVIEK IVEGKLEKFF EEMCLLDQPF IKEPEKKIKD LITEKVAKFG
     ENIMVRRFVR FQVGQTQDE