ID   EFTS_CLOBK              Reviewed;         307 AA.
AC   B1II65;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 74.
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=CLD_2206;
OS   Clostridium botulinum (strain Okra / Type B1).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=498213;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Okra / Type B1;
RX   PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA   Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA   Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT   "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT   and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT   plasmids.";
RL   PLoS ONE 2:E1271-E1271(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; CP000939; ACA46822.1; -; Genomic_DNA.
DR   RefSeq; WP_003384678.1; NC_010516.1.
DR   AlphaFoldDB; B1II65; -.
DR   SMR; B1II65; -.
DR   EnsemblBacteria; ACA46822; ACA46822; CLD_2206.
DR   GeneID; 5186689; -.
DR   KEGG; cbb:CLD_2206; -.
DR   HOGENOM; CLU_047155_0_0_9; -.
DR   OMA; DAGMMDC; -.
DR   Proteomes; UP000008541; 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_1000116716"
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