ID A0A0G0S7S6_9BACT Unreviewed; 151 AA. AC A0A0G0S7S6; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 08-MAY-2019, entry version 16. DE RecName: Full=Elongation factor Ts {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}; RN [1] {ECO:0000313|EMBL:KKR30795.1} 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 RT large 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. {ECO:0000256|HAMAP- CC Rule:MF_00050}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 EnsemblBacteria; KKR30795; KKR30795; UT61_C0002G0039. DR PATRIC; fig|1618552.3.peg.69; -. 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; 1. DR Pfam; PF00889; EF_TS; 1. DR SUPFAM; SSF46934; SSF46934; 1. DR SUPFAM; SSF54713; SSF54713; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00050}; KW Elongation factor {ECO:0000256|HAMAP-Rule:MF_00050, KW ECO:0000313|EMBL:KKR30795.1}; KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00050}. FT DOMAIN 75 148 EF_TS. {ECO:0000259|Pfam:PF00889}. FT REGION 82 85 Involved in Mg(2+) ion dislocation from FT EF-Tu. {ECO:0000256|HAMAP-Rule:MF_00050}. FT COILED 20 40 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 151 AA; 17289 MW; 8A8ED8AB6A66163C CRC64; MTKITVDQIR ELKEDTGAPV MRTKKVLEEL KGDMKKAEEI LRKEGFEKVA KRVRRETSEG IVATYAHHNQ KVVGVIELFC ETDFVARNEL FQNLAHDLAM QVASMGEKDF EKQEFIKDPS KIVEDLVKEV IAKTGENARI GRIFRVELGQ K //