ID   EFTS_AQUAE              Reviewed;         290 AA.
AC   O66930;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Elongation factor Ts;
DE            Short=EF-Ts;
GN   Name=tsf; OrderedLocusNames=aq_715;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(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; AE000657; AAC06887.1; -; Genomic_DNA.
DR   PIR; F70362; F70362.
DR   RefSeq; NP_213490.1; NC_000918.1.
DR   RefSeq; WP_010880428.1; NC_000918.1.
DR   AlphaFoldDB; O66930; -.
DR   SMR; O66930; -.
DR   STRING; 224324.aq_715; -.
DR   PRIDE; O66930; -.
DR   EnsemblBacteria; AAC06887; AAC06887; aq_715.
DR   KEGG; aae:aq_715; -.
DR   PATRIC; fig|224324.8.peg.572; -.
DR   eggNOG; COG0264; Bacteria.
DR   HOGENOM; CLU_047155_0_2_0; -.
DR   InParanoid; O66930; -.
DR   OMA; DAGMMDC; -.
DR   OrthoDB; 1405357at2; -.
DR   Proteomes; UP000000798; 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; 3.
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..290
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_0000161066"
FT   REGION          83..86
FT                   /note="Involved in Mg(2+) ion dislocation from EF-Tu"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   290 AA;  33365 MW;  3C3AF0F0A2170ED9 CRC64;
     MRMAVSMEDV KKLREMTGAG MLDCKKALEE AGGDIEKAKE ILRVKGLAKA EKKAGRETKE
     GLIYVIVSED RKKGAMIELN CETDFVARNE EFRKLAERIT RHILEKDENK NKSGEGSEIL
     SQELYDEPGK TVETLIKEAI AKIGENIRLS RYCRYDTEDY LHSYVHGGGR IGVLLDFKAP
     ELNDQVLRLV QDVAMQIAAM RPEYVRIEDI PQEVLERERR ILREQALQEG KPEHIVDKIV
     EGKLKKFYQE KVLLEQPFIK EEKKQVKDVI KESGLNVEIK RFCRFELGGL