RNA-mediated control of virulence gene expression is widespread among pathogenic bacteria. However, in some major human pathogens such as Streptococcus pneumoniae, its role remains poorly understood. In this study we identify a regulatory function for the 3’-untranslated region (3’UTR) of the mRNA encoding the pneumococcal surface protein A (PspA), a multifunctional surface protein and major virulence factor. Using quantitative proteomics, we identify the protein chaperone Caseinolytic protease L (ClpL) as a regulatory target of the pspA-3’UTR. Downstream analysis reveals that the pspA-3’UTR represses ClpL expression in a temperature-dependent manner. Altogether, this study unveils a riboregulatory role for the pspA mRNA, revealing another layer of PspA-mediated virulence in the human pathogen S. pneumoniae.