ID A0A0G0S7S6_9BACT Unreviewed; 151 AA. AC A0A0G0S7S6; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 03-AUG-2022, entry version 22. DE RecName: Full=Elongation factor Ts {ECO:0000256|ARBA:ARBA00016956, ECO:0000256|HAMAP-Rule:MF_00050}; DE Short=EF-Ts {ECO:0000256|HAMAP-Rule:MF_00050}; GN Name=tsf {ECO:0000256|HAMAP-Rule:MF_00050}; GN ORFNames=UT61_C0002G0039 {ECO:0000313|EMBL:KKR30795.1}; OS Candidatus Woesebacteria bacterium GW2011_GWA1_39_8. OC Bacteria; Candidatus Woesebacteria. OX NCBI_TaxID=1618552 {ECO:0000313|EMBL:KKR30795.1, ECO:0000313|Proteomes:UP000034793}; RN [1] {ECO:0000313|EMBL:KKR30795.1, ECO:0000313|Proteomes:UP000034793} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A., RA Wilkins M.J., Williams K.H., Banfield J.F.; RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large RT radiation of phyla."; RL Nature 0:0-0(2015). 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:0000256|HAMAP-Rule:MF_00050}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00050}. CC -!- SIMILARITY: Belongs to the EF-Ts family. CC {ECO:0000256|ARBA:ARBA00005532, ECO:0000256|HAMAP-Rule:MF_00050}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KKR30795.1}. 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; LBXL01000002; KKR30795.1; -; Genomic_DNA. DR PATRIC; fig|1618552.3.peg.69; -. DR Proteomes; UP000034793; Unassembled WGS sequence. 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; -; 1. 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; IPR009060; UBA-like_sf. DR PANTHER; PTHR11741; PTHR11741; 2. DR Pfam; PF00889; EF_TS; 1. DR SUPFAM; SSF46934; SSF46934; 1. DR SUPFAM; SSF54713; SSF54713; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00050}; KW Elongation factor {ECO:0000256|ARBA:ARBA00022768, ECO:0000256|HAMAP- KW Rule:MF_00050}; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP- KW Rule:MF_00050}. FT DOMAIN 75..148 FT /note="EF_TS" FT /evidence="ECO:0000259|Pfam:PF00889" FT REGION 82..85 FT /note="Involved in Mg(2+) ion dislocation from EF-Tu" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00050" SQ SEQUENCE 151 AA; 17289 MW; 8A8ED8AB6A66163C CRC64; MTKITVDQIR ELKEDTGAPV MRTKKVLEEL KGDMKKAEEI LRKEGFEKVA KRVRRETSEG IVATYAHHNQ KVVGVIELFC ETDFVARNEL FQNLAHDLAM QVASMGEKDF EKQEFIKDPS KIVEDLVKEV IAKTGENARI GRIFRVELGQ K //