Ribosome is a protein translation machine and the target of a variety of clinical antimicrobial drugs. Therefore, in-depth understanding of bacterial protein translation mechanism is of great significance. Translation consists of initiation, elongation, termination, and recycling, coordinating to achieve high fidelity and precise regulation. Translocation is one of the most important events in the process of translation, which requires large conformational changes of the ribosome as well as the precise movement of tRNA2-mRNA through ribosome. In bacteria, translocation is driven by elongation factor G that catalyzes the hydrolysis of GTP. The recent development in single molecule fluorescence resonance energy transfer (smFRET) makes it possible to study tRNA movements and observe the conformational dynamics of the ribosome in real time. Here, we review the recent smFRET study progress in the dynamics of ribosome translocation. These advances will provide much insights into the molecular details and dynamics of the ribosome complexes, shedding new light on the process of translocation.