The prototypic formyl peptide fMet‐Leu‐Phe (fMLF) is an E. coli‐derived chemoattractant for neutrophils. fMLF is a potent agonist of human formyl peptide receptor 1 (FPR1) and induces bactericidal functions of human neutrophils at nanomolar concentrations. However, mouse neutrophil activation requires fMLF concentrations in the micromolar range. To determine whether the mouse FPR is a physiologically relevant receptor for the detection of invading bacteria, formyl peptides derived from S. aureus and L. monocytogenes were examined. It was found that a tetrapeptide (fMIFL) from S. aureus and a pentapeptide (fMIVIL) from L. monocytogenes are potent agonists for the activation of mouse neutrophils. Both fMIFL and fMIVIL induced chemotaxis at concentrations of 1–10 nM and superoxide production at concentrations of 10–100 nM. Additionally, fMIFL and fMIVIL induced greater calcium mobilization than fMLF in mouse neutrophils. Mouse FPR1‐transfected rat basophilic leukemia cells (RBL) also responded to these peptides with greater induction of calcium mobilization and phosphorylation of ERK1/2 compared to fMLF. In conclusion, the S. aureus and L. monocytogenes derived peptides are approximately 100‐fold more potent than fMLF for the mouse FPR1. Differential recognition of formyl peptides from different bacterial strains by mouse neutrophils may be important for the innate immunity to these microorganisms.