ID   EFTS_STRSV              Reviewed;         347 AA.
AC   A3CQW2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=SSA_2202;
OS   Streptococcus sanguinis (strain SK36).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=388919;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK36;
RX   PubMed=17277061; DOI=10.1128/jb.01808-06;
RA   Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P.,
RA   Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D.,
RA   Paik S., Peterson D.L., Macrina F.L., Buck G.A.;
RT   "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL   J. Bacteriol. 189:3166-3175(2007).
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; CP000387; ABN45567.1; -; Genomic_DNA.
DR   RefSeq; WP_002894014.1; NC_009009.1.
DR   RefSeq; YP_001036117.1; NC_009009.1.
DR   AlphaFoldDB; A3CQW2; -.
DR   SMR; A3CQW2; -.
DR   STRING; 388919.SSA_2202; -.
DR   PRIDE; A3CQW2; -.
DR   EnsemblBacteria; ABN45567; ABN45567; SSA_2202.
DR   GeneID; 61535525; -.
DR   KEGG; ssa:SSA_2202; -.
DR   PATRIC; fig|388919.9.peg.2087; -.
DR   eggNOG; COG0264; Bacteria.
DR   HOGENOM; CLU_047155_0_1_9; -.
DR   OMA; DAGMMDC; -.
DR   OrthoDB; 1405357at2; -.
DR   Proteomes; UP000002148; 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; -; 3.
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..347
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_1000006193"
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   347 AA;  37348 MW;  C43A8C2C90AE756E CRC64;
     MAEITAKLVK ELREKSGAGV MDAKKALVET DGDIEKAIEL LREKGMAKAA KKADRVAAEG
     LTGVYVNGNV AAVVEVNAET DFVAKNAQFV DLVNATAKVI AEGKPANNEE ALALTMPSGE
     TLEAAYVSAT ATIGEKISFR RFALIEKTDA QHFGAYQHNG GRIGVISVIE GGDDALAKQI
     SMHIAAMKPT VLSYKELDEQ FVKDELAQLN HVIDQDNESR AMVGKPALPH LKYGSKAQLT
     DAVVAQAEED IKAELAAEGK PEKIWDKIIP GKMDRFMLDN TKVDQAYTLL AQVYIMDDSK
     TVEAYLESVN ASVVEFARFE VGEGIEKAAN DFENEVAATM AAALGQN