ID   EFTS_RICPR              Reviewed;         309 AA.
AC   Q9ZE60;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=Elongation factor Ts;
DE            Short=EF-Ts;
GN   Name=tsf; OrderedLocusNames=RP087;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the EF-Ts family. {ECO:0000305}.
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DR   EMBL; AJ235270; CAA14557.1; -; Genomic_DNA.
DR   PIR; F71717; F71717.
DR   RefSeq; NP_220480.1; NC_000963.1.
DR   RefSeq; WP_004599734.1; NC_000963.1.
DR   AlphaFoldDB; Q9ZE60; -.
DR   SMR; Q9ZE60; -.
DR   STRING; 272947.RP087; -.
DR   EnsemblBacteria; CAA14557; CAA14557; CAA14557.
DR   GeneID; 57569214; -.
DR   KEGG; rpr:RP087; -.
DR   PATRIC; fig|272947.5.peg.87; -.
DR   eggNOG; COG0264; Bacteria.
DR   HOGENOM; CLU_047155_2_0_5; -.
DR   OMA; DAGMMDC; -.
DR   Proteomes; UP000002480; 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..309
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_0000161185"
FT   REGION          82..85
FT                   /note="Involved in Mg(2+) ion dislocation from EF-Tu"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   309 AA;  34080 MW;  28A207A1462CF633 CRC64;
     MSEINISAVV VKELREKTGA GMMDCKKALI ETSGNFEEAI DFLRKKGLAA AVKKSGRIAS
     EGLTAVKVDG LISAVIEVNS ETDFVARNKQ FQDLVKDIVN LAIIAQNIDT LKISKMQSGK
     SVEEEIIDNI AIIGENLTLR RMDILEISNG AIGSYVHNEV VPHLGKISVL VGLESNAKDK
     VKLEALAKQI AVHVAGNNPQ SIDTLSLDKS LIEREKKVFF EKSKEEGKPN HIIEKMVEGR
     IRKFFSEVVL LHQNFLFEPK LTVAEVIKNA EQELSAEIKI TKFIRYALGE GIEHAEKNFA
     DEVAAITQC