ID   EFTS_RHOPA              Reviewed;         308 AA.
AC   P61338;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=RPA2921;
OS   Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=258594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-98 / CGA009;
RX   PubMed=14704707; DOI=10.1038/nbt923;
RA   Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA   Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA   Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA   Harrison F.H., Gibson J., Harwood C.S.;
RT   "Complete genome sequence of the metabolically versatile photosynthetic
RT   bacterium Rhodopseudomonas palustris.";
RL   Nat. Biotechnol. 22:55-61(2004).
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; BX572602; CAE28362.1; -; Genomic_DNA.
DR   RefSeq; WP_011158470.1; NC_005296.1.
DR   AlphaFoldDB; P61338; -.
DR   SMR; P61338; -.
DR   STRING; 258594.RPA2921; -.
DR   PRIDE; P61338; -.
DR   EnsemblBacteria; CAE28362; CAE28362; RPA2921.
DR   GeneID; 66894003; -.
DR   KEGG; rpa:RPA2921; -.
DR   eggNOG; COG0264; Bacteria.
DR   HOGENOM; CLU_047155_2_0_5; -.
DR   OMA; DAGMMDC; -.
DR   PhylomeDB; P61338; -.
DR   BioCyc; RPAL258594:TX73_RS14895-MON; -.
DR   Proteomes; UP000001426; 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; PS01126; EF_TS_1; 1.
DR   PROSITE; PS01127; EF_TS_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Elongation factor; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..308
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_0000161183"
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   308 AA;  32206 MW;  D2DC045AC35DF593 CRC64;
     MATITAAMVK ELRETTGVGM MDCKQALAET DGNIDAAIDW LRKKGLSKAA KKAGRVAAEG
     LIGALTDGTK GVVIEVNSET DFVARNEQFQ GLVKMIAQVA LKVGADLDAI NAAPVGSTTV
     AGAIADAIAT IGENMTLRRA AALSVSQGVV ASYIHNAVID GAGKMGVIVA LESAGKADEL
     AVLGRQLAMH VAAANPQALD PTSLDPAVVQ REREVMADKY RQQGKPENMI EKIVENGLKT
     YYKEVCLLEQ AYIHDEKGKS VAQAVKEAEG KVGAPIKIVG FVRYALGEGI EKQTSDFAAE
     VAAASGQK