Ribosome-dependent ATPase that functions in cytoplasmic translation elongation (PubMed:7657623, PubMed:6456269, PubMed:29300771). Required for the ATP-dependent release of deacylated tRNA from the ribosomal E-site during protein biosynthesis (PubMed:7657623). Stimulates the eEF1A-dependent binding of aminoacyl-tRNA to the ribosomal A-site, which has reduced affinity for tRNA as long as the E-site is occupied (PubMed:7657623). Plays a role as a negative regulator of the GCN2 kinase activity; impairs GCN1-mediated GCN2 activation on ribosomes by reducing GCN1-ribosome affinity, and hence GCN2-mediated eIF-2-alpha phosphorylation in amino acid-starved or repleted cells (PubMed:22888004). ATP + H2O = ADP + H(+) + phosphate Inhibited by the translational inhibitors neomycin and alpha-sarcin, which suppress the ATPase activity. Protein biosynthesis; polypeptide chain elongation. Monomer. Interacts with elongation factor 1A (eEF1A). Interacts through its N-terminus with 18S rRNA. Associates with ribosomes (PubMed:22888004). Increases in strong (1 mM) hydrogen peroxide stress, and decreases in milder (0.5 mM) hydrogen peroxide stress. The heat repeats and the C-terminal domain are necessary for impairing GCN1 function on ribosomes, and hence preventing GCN2 kinase activity in amino acid-starved or repleted cells (PubMed:22888004). Present with 870578 molecules/cell in log phase SD medium. Belongs to the ABC transporter superfamily. ABCF family. EF3 subfamily.