Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. Inhibited by fusidic acid and sordarin, which prevent the release of eEF2 from the ribosome after the translocation step (PubMed:9452424, PubMed:12692531, PubMed:14976550). While fusidic acid acts on all eukaryotic eEF2, sordarin specifically binds and inhibits only selected fungal eEF2 (PubMed:9452424). Protein biosynthesis; polypeptide chain elongation. Binds to 80S ribosomes (PubMed:12692531, PubMed:14976550, PubMed:15316019). Interacts with the 40S ribosomal subunit protein RPL9A; the interaction is direct (PubMed:14976550). Interacts with the 60S ribosomal subunit proteins RPL12A; the interaction is direct (PubMed:14976550). Interacts with RPS23A; the interaction is direct (PubMed:14976550). Interacts with 18S rRNA; the interaction is direct (PubMed:14976550). Interacts with 25S rRNA; the interaction is direct (PubMed:14976550). Interacts with RPL0 (PubMed:12410829). Diphthamide can be ADP-ribosylated by diphtheria toxin and by Pseudomonas exotoxin A, thus abolishing its function. Present with 160782 molecules/cell in log phase SD medium. There are 2 genes for eEF2 in yeast. Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily.