ID   EFTS_CLOBJ              Reviewed;         307 AA.
AC   C1FSK4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 68.
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=CLM_2727;
OS   Clostridium botulinum (strain Kyoto / Type A2).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=536232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kyoto / Type A2;
RA   Shrivastava S., Brinkac L.M., Brown J.L., Bruce D., Detter C.C.,
RA   Johnson E.A., Munk C.A., Smith L.A., Smith T.J., Sutton G., Brettin T.S.;
RT   "Genome sequence of Clostridium botulinum A2 Kyoto.";
RL   Submitted (OCT-2008) 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; CP001581; ACO85612.1; -; Genomic_DNA.
DR   RefSeq; WP_003384678.1; NC_012563.1.
DR   AlphaFoldDB; C1FSK4; -.
DR   SMR; C1FSK4; -.
DR   STRING; 536232.CLM_2727; -.
DR   EnsemblBacteria; ACO85612; ACO85612; CLM_2727.
DR   GeneID; 5186689; -.
DR   KEGG; cby:CLM_2727; -.
DR   eggNOG; COG0264; Bacteria.
DR   HOGENOM; CLU_047155_0_0_9; -.
DR   OMA; DAGMMDC; -.
DR   Proteomes; UP000001374; 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; 3.
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.
PE   3: Inferred from homology;
KW   Cytoplasm; Elongation factor; Protein biosynthesis.
FT   CHAIN           1..307
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_1000189869"
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   307 AA;  34199 MW;  41D51860653FFDC2 CRC64;
     MISAKMVKDL REKTGAGMMD CKKALTECDG DLEKAVEVLR EKGLAAAAKK SGRVAAEGIV
     STYISEDMKN GSIVEFNCET DFVSVNELFV ELANNLSKQA AFSNVSTAEE LLEEKYIADE
     SKLVKDVITE LIAKLGENMN LRRIAKLSVD KGVITSYIHG GGRIGVLVKL ACEKEDAKLA
     EIAKDVAMQV AATNPLFLNR DGVDTDTLEK EKEIYRVQAL NEGKPEKVVE KMVMGRINKY
     YKENCLVEQL WVKNGDYTIT KYLQEQSKEI GADITVEAFV RYEKGEGIEK KEEDFAEEVQ
     RQMNQGK