ID   EFTS_BRUA4              Reviewed;         305 AA.
AC   A6X0J2;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   25-MAY-2022, entry version 77.
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=Oant_2030;
OS   Brucella anthropi (strain ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 /
OS   LMG 3331 / NBRC 15819 / NCTC 12168 / Alc 37) (Ochrobactrum anthropi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=439375;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 / LMG 3331 / NBRC
RC   15819 / NCTC 12168 / Alc 37;
RX   PubMed=21685287; DOI=10.1128/jb.05335-11;
RA   Chain P.S., Lang D.M., Comerci D.J., Malfatti S.A., Vergez L.M., Shin M.,
RA   Ugalde R.A., Garcia E., Tolmasky M.E.;
RT   "Genome of Ochrobactrum anthropi ATCC 49188 T, a versatile opportunistic
RT   pathogen and symbiont of several eukaryotic hosts.";
RL   J. Bacteriol. 193:4274-4275(2011).
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=ABS14746.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000758; ABS14746.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_036578226.1; NC_009667.1.
DR   AlphaFoldDB; A6X0J2; -.
DR   SMR; A6X0J2; -.
DR   STRING; 439375.Oant_2030; -.
DR   EnsemblBacteria; ABS14746; ABS14746; Oant_2030.
DR   GeneID; 61317513; -.
DR   KEGG; oan:Oant_2030; -.
DR   PATRIC; fig|439375.7.peg.2134; -.
DR   eggNOG; COG0264; Bacteria.
DR   HOGENOM; CLU_047155_2_0_5; -.
DR   OrthoDB; 1405357at2; -.
DR   PhylomeDB; A6X0J2; -.
DR   Proteomes; UP000002301; 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; Reference proteome.
FT   CHAIN           1..305
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_0000323459"
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;  31593 MW;  AC46756BD62DC43B CRC64;
     MSISASLVKE LRDLTGAGMM DCKTALAETN GDIEAAVDWL RAKGIAKADK KAGRTAAEGL
     VGVAASGNKA VVVEVNSETD FVARNDAFQD LVRKIAQAAL STDGSTEAVA NANVDGKTVT
     ETAKDAVATI GENIGFRRSA ALTVPQGVVA TYIHNGVADG LGKLGVLVAI ETAGDAEAAN
     AFGRQVAMHV AAINPLALTA EDVDPAAAER EKAIFIEQAR ESGKPDNIIE KMIEGRMRKF
     YEEVVLLSQA FVINPDLTVA AALKEAEKTI GAPAKITGFV RVALGEGIEK EETDFAAEVA
     AAAKG