Ers has been identified in a recent study as a protein involved in the pathogenesis and the stress response of the lactic acid bacterium Enterococcus faecalis, an opportunistic pathogen. In the E. faecalis sequenced genome, Ers is annotated as a transcriptional regulator member of the Crp/Fnr family. This protein has been shown to be involved in the oxidative stress response as well as in the survival within macrophages. In the present study, we sum up the characteristics of Ers and provide further evidence that this protein is a member of the PrfA branch of this regulator family. These features emphasize the importance of studying Ers since PrfA is the major regulator of virulence in Listeria monocytogenes. Ers shares common Crp/Fnr family characteristics, including a HTH motif, a cyclic nucleotide binding domain and conserved amino acid residues. Furthermore, a "PrfA-box-like" sequence has been identified in the ers promoter region. A similar sequence is present in the ef0082 promoter, a gene known to be a member of the Ers regulon. Moreover, ers shares the same genetic neighborhood as other PrfA-like proteins, present in Gram positive bacteria. Lastly, by comparison with PrfA, we have identified an amino acid substitution in the Ers sequence. Such a substitution could imply that Ers is in a constitutively active form.