ID   EFTS_STRP6              Reviewed;         346 AA.
AC   Q5X9J8;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 2.
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=M6_Spy1780;
OS   Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=286636;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-946 / MGAS10394;
RX   PubMed=15272401; DOI=10.1086/422697;
RA   Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E.,
RA   Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.;
RT   "Progress toward characterization of the group A Streptococcus metagenome:
RT   complete genome sequence of a macrolide-resistant serotype M6 strain.";
RL   J. Infect. Dis. 190:727-738(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=AAT87915.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000003; AAT87915.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_002982258.1; NC_006086.1.
DR   AlphaFoldDB; Q5X9J8; -.
DR   SMR; Q5X9J8; -.
DR   EnsemblBacteria; AAT87915; AAT87915; M6_Spy1780.
DR   GeneID; 57853446; -.
DR   KEGG; spa:M6_Spy1780; -.
DR   HOGENOM; CLU_047155_0_1_9; -.
DR   Proteomes; UP000001167; 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.
FT   CHAIN           1..346
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_0000161212"
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;  37257 MW;  8679FD8D573750A1 CRC64;
     MAEITAKLVK ELREKSGAGV MDAKKALVET DGDMDKAVEL LREKGMAKAA KKADRVAAEG
     LTGVYVHGNV AAVVEVNAET DFVAKNAQFV ELVNATAKVI AEGKPANNDE ALALVMPSGE
     TLAEAYVNAT ATIGEKISFR RFALIEKTDE QHFGAYQHNG GRIGVISVVE GGDDALAKQV
     SMHIAAMKPT VLSYTELDAQ FIKDELAQLN HAIELDNESR AMVDKPALPF LKYGSKAQLS
     DDVITAAEAD IKAELAAEGK PEKIWDKIIP GKMDRFMLDN TKVDQAYTLL AQVYIMDDSK
     TVEAYLDSVN AKAIAFARFE VGEGIEKKAN DFESEVAATM AAALNN