ID   EFTS_BRUAB              Reviewed;         305 AA.
AC   Q57CX8;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=BruAb1_1167;
OS   Brucella abortus biovar 1 (strain 9-941).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=262698;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9-941;
RX   PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005;
RA   Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA   Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT   "Completion of the genome sequence of Brucella abortus and comparison to
RT   the highly similar genomes of Brucella melitensis and Brucella suis.";
RL   J. Bacteriol. 187:2715-2726(2005).
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; AE017223; AAX74506.1; -; Genomic_DNA.
DR   RefSeq; WP_002964288.1; NC_006932.1.
DR   AlphaFoldDB; Q57CX8; -.
DR   SMR; Q57CX8; -.
DR   EnsemblBacteria; AAX74506; AAX74506; BruAb1_1167.
DR   GeneID; 45124535; -.
DR   GeneID; 55590842; -.
DR   KEGG; bmb:BruAb1_1167; -.
DR   HOGENOM; CLU_047155_2_0_5; -.
DR   OMA; DAGMMDC; -.
DR   Proteomes; UP000000540; 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..305
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_0000241465"
FT   REGION          79..82
FT                   /note="Involved in Mg(2+) ion dislocation from EF-Tu"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00050"
SQ   SEQUENCE   305 AA;  31491 MW;  6E7660A97411A242 CRC64;
     MSISASLVKE LRDLTGAGMM DCKAALAATE GKIEAAVDWL RAKGIAKADK KAGRTAAEGL
     VGVAASGNKA VVVEVNSETD FVARNDAFQE LVRKIAQAAL STDGSSEAVA NANVDGKTVT
     EAAKDAVATI GENISFRRSA ALSVPQGVVA TYIHNGVADG LGKLGVLVAI ETAGDAEAAQ
     AFGRQVAMHV AAVNPLALTS ADVNPEAAER EKAIFIDQAR QSGKPDNIIE KMVEGRMRKF
     YEEVVLLSQA FVINPDLTVE AALKDAEKAI GAPAKITGFA RIALGEGIEK EESDFAAEVA
     AAAKG