ID   EFTS_STRT2              Reviewed;         346 AA.
AC   Q5M6G4;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 2.
DT   25-MAY-2022, entry version 102.
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=stu0074;
OS   Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=264199;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-250 / LMG 18311;
RX   PubMed=15543133; DOI=10.1038/nbt1034;
RA   Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D.,
RA   Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M.,
RA   Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D.,
RA   Hancy F., Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.;
RT   "Complete sequence and comparative genome analysis of the dairy bacterium
RT   Streptococcus thermophilus.";
RL   Nat. Biotechnol. 22:1554-1558(2004).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAV59803.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000023; AAV59803.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_002949105.1; NC_006448.1.
DR   AlphaFoldDB; Q5M6G4; -.
DR   SMR; Q5M6G4; -.
DR   STRING; 264199.stu0074; -.
DR   EnsemblBacteria; AAV59803; AAV59803; stu0074.
DR   GeneID; 66898005; -.
DR   KEGG; stl:stu0074; -.
DR   eggNOG; COG0264; Bacteria.
DR   HOGENOM; CLU_047155_0_1_9; -.
DR   Proteomes; UP000001170; 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..346
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_0000241537"
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   346 AA;  37359 MW;  D8FC6F9B580A7CB4 CRC64;
     MAEITAKLVK ELREKSGAGV MDAKKALVEV DGDIEKAIEL LREKGMAKAA KKADRIAAEG
     LTGIYVSGNV AAVVEVNAET DFVAKNAQFV ELVNETAKVI AEGKPANNEE ALALTMPSGE
     TLEAAYVTAT ATIGEKISLR RFAVVEKTDA QHFGAYQHNG GRIGVVSVIE GGDEAIAKQI
     SMHIAAMKPT VLSYSELDEQ FVKDELAQLN HAIDQDNESR AMVNKPALPH LKYGSKAQLT
     DEVIAQAEED IKAELAAEGK PEKIWDKIIP GKMDRFILDN TKVDQAYTLL AQVYIMDDSK
     TVEAYLESVN ASVVEFVRFE VGEGIEKASN DFESEVAATM AAALNN