ID   EFTS_BURCM              Reviewed;         293 AA.
AC   Q0BE16;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 85.
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=Bamb_2051;
OS   Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia
OS   (strain AMMD)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=339670;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-244 / AMMD;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K.,
RA   Ramette A., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD.";
RL   Submitted (AUG-2006) 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; CP000440; ABI87607.1; -; Genomic_DNA.
DR   RefSeq; WP_006752150.1; NZ_CP009798.1.
DR   AlphaFoldDB; Q0BE16; -.
DR   SMR; Q0BE16; -.
DR   STRING; 339670.Bamb_2051; -.
DR   EnsemblBacteria; ABI87607; ABI87607; Bamb_2051.
DR   GeneID; 44692710; -.
DR   GeneID; 60997112; -.
DR   KEGG; bam:Bamb_2051; -.
DR   PATRIC; fig|339670.21.peg.2892; -.
DR   eggNOG; COG0264; Bacteria.
DR   OMA; DAGMMDC; -.
DR   Proteomes; UP000000662; Chromosome 1.
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_1000006063"
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;  31040 MW;  D6F7F9457AFD0C5E CRC64;
     MAAITASMVA ELRAKTDAPM MECKKALTEA DGDLAKAEEL LRVKLGNKAS KAASRVTAEG
     VVASFVGGNA GALVELNCET DFVAKNDDFL AFSKTVAELV ATQNPADVAA LSALPLEGST
     VDAVRLALIG KIGENVSIRR FVRFETANKI ATYLHGARIG VIVEYTGADE QVGKDVAMHI
     AAMKPVALSS ADVPAELIDT ERRVAEQKAA ESGKPAEIVA KMVDGSVQKY LKEVSLLNQT
     FVKNDKQTIE QMLKAANSTV QKFALFVVGE GIEKRQDDFA AEVAAQVAAA KQQ