ID   EFTS_SYNC1              Reviewed;         303 AA.
AC   Q3A396;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 92.
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=Pcar_1920;
OS   Syntrophotalea carbinolica (strain DSM 2380 / NBRC 103641 / GraBd1)
OS   (Pelobacter carbinolicus).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Syntrophotaleaceae; Syntrophotalea.
OX   NCBI_TaxID=338963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2380 / NBRC 103641 / GraBd1;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chertkov O., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Pelobacter carbinolicus DSM 2380.";
RL   Submitted (OCT-2005) 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; CP000142; ABA89161.1; -; Genomic_DNA.
DR   RefSeq; WP_011341666.1; NC_007498.2.
DR   AlphaFoldDB; Q3A396; -.
DR   SMR; Q3A396; -.
DR   STRING; 338963.Pcar_1920; -.
DR   EnsemblBacteria; ABA89161; ABA89161; Pcar_1920.
DR   KEGG; pca:Pcar_1920; -.
DR   eggNOG; COG0264; Bacteria.
DR   HOGENOM; CLU_047155_0_0_7; -.
DR   OMA; DAGMMDC; -.
DR   OrthoDB; 1405357at2; -.
DR   Proteomes; UP000002534; 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; -; 2.
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; 2.
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..303
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_0000241504"
FT   REGION          79..82
FT                   /note="Involved in Mg(2+) ion dislocation from EF-Tu"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00050"
SQ   SEQUENCE   303 AA;  32601 MW;  FD3EDFBD6ACDE103 CRC64;
     MKITASMVSE LRTKTGAGMM DCKKALSEAD GNIEEAVDIL RKKGLSAAAK KADRAAAEGL
     VVGLNEGSCG VLVEVNAETD FVAKNANFQE FTNGVAKVVV SSKPADLEAL KALPFPGTDR
     TVAEEQTHQI ATIGENINLR RFVCFDVAQG AVAVYIHGVG KIGVLVELET SKGDDERVAA
     LGRNLAMHIA AANPQYLNRD EVSAEVVEKE KEIMRTKALE SGKPEKIVEK IIAGQINKYF
     GEVCLLEQAY VIDPDLTVTK VVENLGKEIG AEVTLSRYVR FQLGEGLEKR SDDFAAEVAS
     MTK