ID   EFTS_ACIAC              Reviewed;         298 AA.
AC   A1TN70;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 84.
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=Aave_1824;
OS   Acidovorax citrulli (strain AAC00-1) (Acidovorax avenae subsp. citrulli).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=397945;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAC00-1;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT   "Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1.";
RL   Submitted (DEC-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; CP000512; ABM32408.1; -; Genomic_DNA.
DR   RefSeq; WP_011794954.1; NC_008752.1.
DR   AlphaFoldDB; A1TN70; -.
DR   SMR; A1TN70; -.
DR   STRING; 397945.Aave_1824; -.
DR   EnsemblBacteria; ABM32408; ABM32408; Aave_1824.
DR   KEGG; aav:Aave_1824; -.
DR   eggNOG; COG0264; Bacteria.
DR   HOGENOM; CLU_047155_0_2_4; -.
DR   OMA; DAGMMDC; -.
DR   OrthoDB; 1405357at2; -.
DR   Proteomes; UP000002596; 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; 2.
DR   TIGRFAMs; TIGR00116; tsf; 1.
DR   PROSITE; PS01127; EF_TS_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Elongation factor; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..298
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_1000006042"
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   298 AA;  31199 MW;  B6F6DC36938B20A2 CRC64;
     MAAITASMVA ELRAKTDAPM MECKKALTEA DGDLAKAEEL LRVKLGTKAG KAAARITAEG
     VVASFIEGTT GALIEVNSET DFVSKNDSFI ALAKAAAELV AKHNPADVEA LGALPYSQES
     FGPTLEEVRK GLIGKIGENM SFRRFKRFSG SKLASYLHGT RIGVVVEFDG DETAAKDVAM
     HIAAMKPVAL TSADVPAELI EKERTVAAAK AAESGKPADI AAKMVEGSVQ KYLKEVSLFD
     QVFVKAADGK QTVGQMLKAA NTTVKGFTLY VVGEGIEKKV DDFAAEVAAQ VAAAKAAA