ID   EFTS_RHOBA              Reviewed;         326 AA.
AC   Q7UKH3;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 99.
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=RB10640;
OS   Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC   Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Rhodopirellula.
OX   NCBI_TaxID=243090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX   PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA   Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA   Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA   Reinhardt R.;
RT   "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT   1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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; BX294152; CAD76891.1; -; Genomic_DNA.
DR   RefSeq; NP_869530.1; NC_005027.1.
DR   RefSeq; WP_007325915.1; NC_005027.1.
DR   AlphaFoldDB; Q7UKH3; -.
DR   SMR; Q7UKH3; -.
DR   STRING; 243090.RB10640; -.
DR   EnsemblBacteria; CAD76891; CAD76891; RB10640.
DR   KEGG; rba:RB10640; -.
DR   PATRIC; fig|243090.15.peg.5140; -.
DR   eggNOG; COG0264; Bacteria.
DR   HOGENOM; CLU_047155_0_1_0; -.
DR   InParanoid; Q7UKH3; -.
DR   OMA; EGCVLAK; -.
DR   OrthoDB; 1405357at2; -.
DR   Proteomes; UP000001025; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR   GO; GO:0006414; P:translational elongation; IBA:GO_Central.
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; 2.
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..326
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_0000161182"
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   326 AA;  35755 MW;  41FB2D630D2E5AD7 CRC64;
     MTTISAKAVS ELRKSTGAGM MDCKKALEES GGDLDGAMDY LRKKGQKVAA KRADREASEG
     VVAAVVEGNK GLLLSLGCET DFVAKNEAFI ELTNTIAKMA FDADCKTIDD VNALEIDGTT
     VKERLVNETG KVGEKIEVTN LEVVEGENLA SYIHAGAKIG VLVSYKDGAK DDADQFFRGV
     SMHIAAMKPS ILHPNEFDEE FVQKETEALQ AQINAENELN EKENLGKPMK NVPQFASRRQ
     LTPEVLAATE EAIKEELKAE GKPEKIWDKI VPGKLERFIA DNTLLDQERC LLSQFYALDD
     TKTVEAAIKE FHPEAEVVAF KRISVN