ID   EFTS_BURM9              Reviewed;         293 AA.
AC   A2SB73;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   03-AUG-2022, entry version 78.
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};
GN   OrderedLocusNames=BMA10229_A3256;
OS   Burkholderia mallei (strain NCTC 10229).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=412022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 10229;
RX   PubMed=20333227; DOI=10.1093/gbe/evq003;
RA   Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA   Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA   Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA   Nierman W.C.;
RT   "Continuing evolution of Burkholderia mallei through genome reduction and
RT   large-scale rearrangements.";
RL   Genome Biol. Evol. 2:102-116(2010).
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=ABN00663.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000546; ABN00663.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_004197087.1; NC_008836.1.
DR   AlphaFoldDB; A2SB73; -.
DR   SMR; A2SB73; -.
DR   EnsemblBacteria; ABN00663; ABN00663; BMA10229_A3256.
DR   GeneID; 56595943; -.
DR   KEGG; bml:BMA10229_A3256; -.
DR   HOGENOM; CLU_047155_0_2_4; -.
DR   OMA; DAGMMDC; -.
DR   Proteomes; UP000002283; Chromosome I.
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; PS01127; EF_TS_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Elongation factor; Protein biosynthesis.
FT   CHAIN           1..293
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_0000323444"
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   293 AA;  31193 MW;  1C20211E01F3EC8E CRC64;
     MAAITASMVA ELRAKTDAPM MECKKALTEA DGDMAKAEEL LRVKLGNKAS KAASRVTAEG
     VVASFVGANA GALVELNCET DFVAKNDDFN AFAKTVAELV ATQNPADVAA LSALPLDGKT
     VDEVRLALVG KIGENISIRR FVRFETSNKL ATYLHGSRIG VIVEYTGAQE QVGKDVAMHV
     AAMKPVSLSA DEVPADLIEK ERRVAEQKAA ESGKPAEIVA KMVDGSVQKF LKEVSLLNQP
     FVKNDKQTIE QMLKAADAAV QKFALFVVGE GIEKRQDDFA AEVAAQVAAA KQQ