Pheromone peptides are an important component of bacterial quorum-sensing system. The pheromone peptide cOB1 (VAVLVLGA) of native commensal Enterococcus faecalis has also been identified as an antimicrobial peptide (AMP) and reported to kill the prototype clinical isolate strain of E. faecalis V583. In this study， the pheromone peptide cOB1 has shown to form amyloid-like structures， a characteristic which is never reported for a pheromone peptide so far. With in silico analysis， the peptide was predicted to be highly amyloidogenic. Further， under experimental conditions， cOB1 formed aggregates displaying characteristics of amyloid structures such as bathochromic shift in Congo red absorbance， enhancement in thioflavin T fluorescence， and fibrillar morphology under transmission electron microscopy. This novel property of pheromone peptide cOB1 may have some direct effects on the binding of the pheromone to the receptor cells and subsequent conjugative transfer， making this observation more important for the therapeutics， dealing with the generation of virulent and multidrug-resistant pathogenic strains.