ID   EFTS_FLAJ1              Reviewed;         320 AA.
AC   A5FJI4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=Fjoh_1609;
OS   Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / NBRC
OS   14942 / NCIMB 11054 / UW101) (Cytophaga johnsonae).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=376686;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17061 / DSM 2064 / JCM 8514 / NBRC 14942 / NCIMB 11054 / UW101;
RX   PubMed=19717629; DOI=10.1128/aem.01495-09;
RA   McBride M.J., Xie G., Martens E.C., Lapidus A., Henrissat B., Rhodes R.G.,
RA   Goltsman E., Wang W., Xu J., Hunnicutt D.W., Staroscik A.M., Hoover T.R.,
RA   Cheng Y.Q., Stein J.L.;
RT   "Novel features of the polysaccharide-digesting gliding bacterium
RT   Flavobacterium johnsoniae as revealed by genome sequence analysis.";
RL   Appl. Environ. Microbiol. 75:6864-6875(2009).
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; CP000685; ABQ04641.1; -; Genomic_DNA.
DR   RefSeq; WP_012023685.1; NZ_MUGZ01000017.1.
DR   AlphaFoldDB; A5FJI4; -.
DR   SMR; A5FJI4; -.
DR   STRING; 376686.Fjoh_1609; -.
DR   EnsemblBacteria; ABQ04641; ABQ04641; Fjoh_1609.
DR   KEGG; fjo:Fjoh_1609; -.
DR   eggNOG; COG0264; Bacteria.
DR   HOGENOM; CLU_047155_0_1_10; -.
DR   OMA; EGCVLAK; -.
DR   OrthoDB; 1405357at2; -.
DR   Proteomes; UP000006694; 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; 2.
DR   SUPFAM; SSF46934; SSF46934; 1.
DR   SUPFAM; SSF54713; SSF54713; 2.
DR   TIGRFAMs; TIGR00116; tsf; 1.
DR   PROSITE; PS01126; EF_TS_1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Elongation factor; Protein biosynthesis.
FT   CHAIN           1..320
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_1000074863"
FT   REGION          82..85
FT                   /note="Involved in Mg(2+) ion dislocation from EF-Tu"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00050"
SQ   SEQUENCE   320 AA;  34843 MW;  81B15F4065A3BB7D CRC64;
     MSTITAADVN KLRQSTGAGM MDCKKALVEA EGDFDKAIQI LREKGQKVAA NRSDRESSEG
     AAVSFINADN TKGAIITLNC ETDFVGKNEA FVTLAKDLVE RAINFSNKEE FLASDFNGIT
     VAEKLIEQTG VIGEKIEIGG FEILEGAFVG SYVHVNKIAA LTAISAPIAN AETLTKDVSM
     QVASMGADTL SYKDFDPAFV ESELAARIAV IEKDNEEAKR LGKTLKNVPK YISFSQLTPE
     VIKQAEEDAK AELKAEGKPE QIWDKILPGK VQRFISDNTT LDQEKALLDQ NFIKDDSKKV
     GDYVKGFNVE ITGFKRVTLG