ID   EFTS_STRMU              Reviewed;         348 AA.
AC   Q8DS12;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=SMU_2031;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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; AE014133; AAN59634.1; -; Genomic_DNA.
DR   RefSeq; NP_722328.1; NC_004350.2.
DR   RefSeq; WP_002262346.1; NC_004350.2.
DR   AlphaFoldDB; Q8DS12; -.
DR   SMR; Q8DS12; -.
DR   STRING; 210007.SMU_2031; -.
DR   PRIDE; Q8DS12; -.
DR   EnsemblBacteria; AAN59634; AAN59634; SMU_2031.
DR   KEGG; smu:SMU_2031; -.
DR   PATRIC; fig|210007.7.peg.1811; -.
DR   eggNOG; COG0264; Bacteria.
DR   HOGENOM; CLU_047155_0_1_9; -.
DR   OMA; DAGMMDC; -.
DR   PhylomeDB; Q8DS12; -.
DR   Proteomes; UP000002512; 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; 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..348
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_0000161207"
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   348 AA;  37719 MW;  81239E4C58D5E636 CRC64;
     MANITAALVK ELREKTGAGV MDAKKALVEV EGDMGKAIEL LREKGMAKAA KKADRVAAEG
     LTGVYVDGNV AAIVEVNAET DFVAKNAQFV DLVNETAKVI AEGKPANNEE ALALKTAAGD
     TLEAAYVNAT ATIGEKISFR RFALVEKADK QVFGAYQHNG GKIGVITVLE GENTDEALAK
     QLAMHVAAMN PSVLSYKELS EEFIHDELAQ MNHKIEQDNE SRAMVDKPAL PLLKYGSKGQ
     LTDEVVAQAE EDIKAELKAE GKPEKIWDKI IPGKMARFFL DNTKVDQQYT LLSQVYIMDD
     SKTVEAYMES VNGKVISFVR FEVGEGIEKA ANDFENEVAA TMAAALNK