Bacteria use RNA-binding proteins (RBPs) to express and regulate genes. Despite decades of studies on bacterial genetics and physiology, there are still proteins whose function is unknown. We used two proteomics approaches to uncover a repertoire of RBPs in the pathogenic bacterium S. pyogenes: Orthogonal Organic Phase Purification (OOPS) and RNA Binding Sites Identification (RBS-ID). The combination of these approaches enabled us to identify most of the annotated RBPs. However, the function of a number of identified RNA-interacting proteins is unknown. One of these proteins - YebC - has been selected for further study. YebC is a highly conserved protein present in almost all organisms. The deletion of yebC moderately affects the growth, transcriptome and proteome of S. pyogenes. Interestingly, expression of the secreted protease SpeB is inhibited in the yebC deletion strain. The site-directed mutagenesis performed in S. pyogenes identified several mutations that inactivate the protein without significantly affecting its stability. According to the results of the iCLIP experiment, YebC cross-links with helix 89 of the 23S rRNA near the peptidyl-transferase centre. However, the protein does not stably associate with ribosomes. We performed a ribosome profiling experiment and detected increased pausing at and downstream of the PPP, PPG, PIP and DIP amino acid stretches. Further results obtained with in vivo reporters and an in vitro translation system suggest that YebC is a novel translation factor that alleviates ribosome stalling at the polyproline stretches. Future studies will aim to elucidate the mechanism of action of YebC.