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EFTS_TERTT
ID   EFTS_TERTT              Reviewed;         293 AA.
AC   C5BQF7;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 61.
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=TERTU_1006;
OS   Teredinibacter turnerae (strain ATCC 39867 / T7901).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Teredinibacter.
OX   NCBI_TaxID=377629;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39867 / T7901;
RX   PubMed=19568419; DOI=10.1371/journal.pone.0006085;
RA   Yang J.C., Madupu R., Durkin A.S., Ekborg N.A., Pedamallu C.S.,
RA   Hostetler J.B., Radune D., Toms B.S., Henrissat B., Coutinho P.M.,
RA   Schwarz S., Field L., Trindade-Silva A.E., Soares C.A.G., Elshahawi S.,
RA   Hanora A., Schmidt E.W., Haygood M.G., Posfai J., Benner J., Madinger C.,
RA   Nove J., Anton B., Chaudhary K., Foster J., Holman A., Kumar S.,
RA   Lessard P.A., Luyten Y.A., Slatko B., Wood N., Wu B., Teplitski M.,
RA   Mougous J.D., Ward N., Eisen J.A., Badger J.H., Distel D.L.;
RT   "The complete genome of Teredinibacter turnerae T7901: an intracellular
RT   endosymbiont of marine wood-boring bivalves (shipworms).";
RL   PLoS ONE 4:E6085-E6085(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; CP001614; ACR13743.1; -; Genomic_DNA.
DR   RefSeq; WP_015819858.1; NC_012997.1.
DR   AlphaFoldDB; C5BQF7; -.
DR   SMR; C5BQF7; -.
DR   STRING; 377629.TERTU_1006; -.
DR   EnsemblBacteria; ACR13743; ACR13743; TERTU_1006.
DR   KEGG; ttu:TERTU_1006; -.
DR   eggNOG; COG0264; Bacteria.
DR   HOGENOM; CLU_047155_0_2_6; -.
DR   OMA; DAGMMDC; -.
DR   OrthoDB; 1405357at2; -.
DR   Proteomes; UP000009080; 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..293
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_1000202254"
FT   REGION          81..84
FT                   /note="Involved in Mg(2+) ion dislocation from EF-Tu"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00050"
SQ   SEQUENCE   293 AA;  31089 MW;  AAFECC96A1204741 CRC64;
     MAVSASLVKE LRERTGLGMM ECKKALAETD GDIDAAIENL RKASGLKAAK KADRTAAEGV
     VAAKVADDGS YGVLVEVNSE TDFVARDAGF LAFVDSVVEK AFSAKAADVA AVNDEAMEST
     RQALVQKIGE NIGIRRVSLI EADGGLVGAY VHSNNRIAVM VQLANGGSVE LAKDVAMHIA
     AVNPQVVNPE DMPEEVVNKE KDIIKAQPDM EGKPEQIVEK MMTGRINKFL KENSLVEQPF
     VKDPEITVGA LVKKEGASVV SFSRFEVGEG IEKKEEDFAA EVAAQVAASK GNA
 
 
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