ID   EFTS_RALSO              Reviewed;         292 AA.
AC   Q8XZJ0;
DT   10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2002, sequence version 2.
DT   25-MAY-2022, entry version 110.
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=RSc1405;
GN   ORFNames=RS05287;
OS   Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=267608;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GMI1000;
RX   PubMed=11823852; DOI=10.1038/415497a;
RA   Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA   Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA   Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA   Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA   Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT   "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL   Nature 415:497-502(2002).
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=CAD15107.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AL646052; CAD15107.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011001354.1; NC_003295.1.
DR   AlphaFoldDB; Q8XZJ0; -.
DR   SMR; Q8XZJ0; -.
DR   STRING; 267608.RSc1405; -.
DR   EnsemblBacteria; CAD15107; CAD15107; RSc1405.
DR   GeneID; 60500928; -.
DR   KEGG; rso:RSc1405; -.
DR   eggNOG; COG0264; Bacteria.
DR   HOGENOM; CLU_047155_0_2_4; -.
DR   OMA; DAGMMDC; -.
DR   Proteomes; UP000001436; 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..292
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_0000161179"
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   292 AA;  31135 MW;  07C788FBD7285306 CRC64;
     MAAITASMVA ELRAKTDAPM MECKKALTEA EGNMEKAEEI LRVKLGNKAG KAAARITAEG
     VIASFIDGTI GALVELNCET DFVSRNDDFL GFANEIAKLI ATQNPADVAA LSALSIGDET
     VEAVRTRLIG KIGENMTIRR FQRFEGTKLA SYLHGTRIGV MVAFDGDEVA AKDVAMHAAA
     MKPVALSSDE VPAELIAKER SIAEQKAAES GKPAEIVAKM VEGSVQKYLK EVSLLNQPFV
     KNDKQTVEQM LKAANTTVKG FTLFVVGEGI EKKQDDFAAE VAAQVAAAKQ QA