ID   EFTS_STRRA              Reviewed;         278 AA.
AC   Q9X5Z9;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Elongation factor Ts;
DE            Short=EF-Ts;
GN   Name=tsf;
OS   Streptomyces ramocissimus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1925;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 27529 / CBS 190.69;
RX   PubMed=10517582; DOI=10.1099/00221287-145-9-2293;
RA   Hoogvliet G., van Wezel G.P., Kraal B.;
RT   "Evidence that a single EF-Ts suffices for the recycling of multiple and
RT   divergent EF-Tu species in Streptomyces coelicolor A3(2) and Streptomyces
RT   ramocissimus.";
RL   Microbiology 145:2293-2301(1999).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF130345; AAD34362.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9X5Z9; -.
DR   SMR; Q9X5Z9; -.
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.
FT   CHAIN           1..278
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_0000161214"
FT   REGION          82..85
FT                   /note="Involved in Mg(2+) ion dislocation from EF-Tu"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   278 AA;  29893 MW;  6BDB09BEFFC380DF CRC64;
     MANYTAADVK KLRELTGAGM MDCKKALDEA EGNVEKAVEA LRIKGQKGVA KREGRSAENG
     AVVSIIADDN SSGVLVELKC ETDFVAKGEK FQNVATAIAE HVAKAAPADL DALLASEIEA
     GKTVQAFVDE ANANLGEKIV LDRFAQFADG YVLAYMHRTM PDLPPQIGVL VELDKPNAEV
     AKGVAQHIAA FAPKYLSKED VRPDVVESER RIAEETTRAE GKPEAAIAKI VEGRVNGFFK
     DATLLGQPYA LDNKKSVQKV LDEAGVTLKR FTRIKVGI