ID   EFTS_BARBK              Reviewed;         307 AA.
AC   Q8RT66; A1USE0;
DT   28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 106.
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}; Synonyms=eftS;
GN   OrderedLocusNames=BARBAKC583_0584;
OS   Bartonella bacilliformis (strain ATCC 35685 / NCTC 12138 / KC583).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=360095;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Minnick M.F., Choquette L.E.;
RT   "Translational machinery operon from Bartonella bacilliformis.";
RL   Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35685 / NCTC 12138 / KC583;
RA   Hendrix L., Mohamoud Y., Radune D., Shvartsbeyn A., Daugherty S.,
RA   Dodson R., Durkin A.S., Harkins D., Huot H., Kothari S.P., Madupu R.,
RA   Li J., Nelson W.C., Shrivastava S., Giglio M.G., Haft D., Selengut J.,
RA   Fraser-Ligget C., Seshadri R.;
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; AF469610; AAL82405.1; -; Genomic_DNA.
DR   EMBL; CP000524; ABM45297.1; -; Genomic_DNA.
DR   RefSeq; WP_005766749.1; NC_008783.1.
DR   AlphaFoldDB; Q8RT66; -.
DR   SMR; Q8RT66; -.
DR   STRING; 360095.BARBAKC583_0584; -.
DR   EnsemblBacteria; ABM45297; ABM45297; BARBAKC583_0584.
DR   KEGG; bbk:BARBAKC583_0584; -.
DR   PATRIC; fig|360095.6.peg.569; -.
DR   eggNOG; COG0264; Bacteria.
DR   HOGENOM; CLU_047155_2_0_5; -.
DR   OMA; DAGMMDC; -.
DR   OrthoDB; 1405357at2; -.
DR   Proteomes; UP000000643; 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..307
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_0000161079"
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   307 AA;  32399 MW;  230EF34DE699FBC4 CRC64;
     MSITAAQVKE LRELSGAGMM DCKAALMETN GDIETAVDWL RKKGMAKADK KAGRTAAEGL
     IGIASKGLSA VVVEVNSETD FVARNDAFQT IVRNVATAAL DTEGSVESVS ASIYPGSEKT
     VEEAIKDAIG TIGENMAFRR SAKLSVQNGA VATYIHNSVA DGLGKLGVLV GIETTGDKEV
     AVDFARKVAM HIAATNPLAL TVADVDASIV EREKAIFSDQ ARQSGKPENI IEKMVEGRIR
     KFYEEVVLLS QAFVMNPDVT VEASLKDAEK MIGAPAKITG FVRFALGEGV EKEEVDFAAE
     VAAAAKG