EFTS_FRATM
ID EFTS_FRATM Reviewed; 289 AA.
AC B2SDZ6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
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=FTM_1538;
OS Francisella tularensis subsp. mediasiatica (strain FSC147).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=441952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSC147;
RX PubMed=19521508; DOI=10.1371/journal.ppat.1000472;
RA Larsson P., Elfsmark D., Svensson K., Wikstroem P., Forsman M., Brettin T.,
RA Keim P., Johansson A.;
RT "Molecular evolutionary consequences of niche restriction in Francisella
RT tularensis, a facultative intracellular pathogen.";
RL PLoS Pathog. 5:E1000472-E1000472(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}.
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; CP000915; ACD31360.1; -; Genomic_DNA.
DR RefSeq; WP_003017693.1; NC_010677.1.
DR AlphaFoldDB; B2SDZ6; -.
DR SMR; B2SDZ6; -.
DR KEGG; ftm:FTM_1538; -.
DR HOGENOM; CLU_047155_0_2_6; -.
DR OMA; DAGMMDC; -.
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..289
FT /note="Elongation factor Ts"
FT /id="PRO_1000116740"
FT REGION 80..83
FT /note="Involved in Mg(2+) ion dislocation from EF-Tu"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00050"
SQ SEQUENCE 289 AA; 30960 MW; 81DA026C11E44C09 CRC64;
MSNISAKLVK ELRERTGAGM MECKKALVAA AGDIEKAAEE MRISGQAKAD KKASRVAAEG
VIEVYAADGR AILLEINSET DFVARDETFK KFAQEAVKAA HAANAKTIEE VLAAKTSNGE
TVEEARKSLI AKIGENIQVR RVKTVEAETL GAYIHGSKIG VVAALEGGDE DLAKDVAMHV
AAANPMVVSG DQVPADVVAK EKEIFTAQAK ESGKPAEIIE KMIVGRIRKF LDEVALLGQD
FVKDPAIKVE KLVKDKGAKV VNFIRLDVGE GIEKKEEDFA AEVMSQIKG