This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. May play an important regulatory role in cell growth and in the bacterial response to nutrient deprivation. Plays a stimulatory role in trans-translation; binds tmRNA. Protects glycyl-tRNA(Gly) from hydrolysis by E.coli D-aminoacyl-tRNA deacylase (dtd) (By similarity). (Microbial infection) Upon infection by bacteriophage Qbeta, part of the viral RNA-dependent RNA polymerase complex. With EF-Ts may provide a stabilizing scaffold for the beta (catalytic) subunit. Helps separate the double-stranded RNA of the template and growing RNA during elongation. With the beta subunit helps form the exit tunnel for template RNA. (Microbial infection) Required for the tRNase activity of CdiA-CT from E.coli strain EC869; the toxic CT module is thought to cleave tRNA in the context of translationally active GTP EF-Tu-aa-tRNA complexes. GTP is required for tRNase activity but is not hydrolyzed. CdiA-CT is the toxic component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria in a contact-dependent fashion (PubMed:28223500). EF-Tu interacts with at least 2 different toxic CT domains, the 2 toxins are different and degrade tRNA at different positions (PubMed:28973472, PubMed:28223500). (Microbial infection) Required for the tRNase activity of CdiA-CT from E.coli strain NC101; the toxic CT module is thought to cleave tRNA in the context of translationally active GTP EF-Tu-aa-tRNA complexes. The toxin may remodel the EF-Tu-aa-tRNA complex to displace the 3'-end of the aa-tRNA so it can enter the toxin active site and be cleaved. GTP is required for tRNase activity but is not hydrolyzed. CdiA-CT is the toxic component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria in a contact-dependent fashion (PubMed:28223500). EF-Tu interacts with at least 2 different toxic CT domains, the 2 toxins are different and degrade tRNA at different positions (PubMed:28973472, PubMed:28223500). Monomer. Heterotetramer composed of two EF-Ts.EF-Tu dimer complexes (By similarity). (Microbial infection) Upon infection by bacteriophage Qbeta, part of the viral RNA-dependent RNA polymerase complex, the other subunits are the viral replicase catalytic subunit (AC P14647), host ribosomal protein S1 and EF-Ts (PubMed:816798). (Microbial infection) Forms a contact-dependent growth inhibition complex of EF-Tu, CdiA-CT-EC869 and CdiI-EC869 as well as a GTP, EF-Tu, CdiA-CT-EC869 complex. (Microbial infection) Forms a contact-dependent growth inhibition complex of CdiA-CT-NC101, CdiI-NC101 and EF-Tu; the complex is a dimer of heterotrimers. Between 50-80% of the protein is associated with the cell inner membrane. Localization to the membrane has been suggested to follow nutrient stress. The N-terminus is blocked. Methylated in vivo on Lys-57 in response to nutrient starvation. Phosphorylated in vitro by phage protein doc on Thr-383. Phosphorylated in vitro by HipA on Thr-383 (PubMed:19150849), this has since been reported not to occur in vivo (PubMed:24095282). Present with about 70,000 molecules/cell. This chain is also used in bacteriophage Q-beta RNA polymerase. The antibiotic kirromycin inhibits protein biosynthesis by inhibiting the release of EF-Tu from the ribosome. The antibiotic pulvomycin inhibits protein biosynthesis by disrupting the allosteric control mechanism of EF-Tu. Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily. EF-Tu 1 and EF-Tu 2 differ in a single position and are no longer merged. However, many papers are found in both entries as it is not always possible to determine for each paper which of EF-Tu 1 or EF-Tu 2 was being worked upon.