Staphylococcus aureus remains to be one of the most concerning bacterial pathogens, with its capability to adapt host immune systems and antibiotic attacks. Treatment of severe infections caused by methicillin-resistant S. aureus (MRSA) relies on last-line antibiotics, including daptomycin. Daptomycin targets bacterial cell membrane for its bactericidal effects, with a mechanism thought to be similar to host cationic antimicrobial peptides (CAMPs). The rise of daptomycin resistance (DAP-R) is alarming and is often associated with persistent and complicated infections. Nonsynonymous mutations in multiple peptide resistance factor (mprF) have been highly associated with DAP-R. MprF is a bifunctional enzyme to synthesize lysyl-phosphatidylglycerol (L-PG) and translocate L-PG from the inner leaflet to the outer leaflet of cell membranes. S. aureus relies on MprF to defend attacks from host CAMPs. How these mprF mutations lead to DAP-R is not entirely clear. Here, we characterized the full repertoire of mprF mutations within 10,000 DAP-R clones. We identified 24 nonsynonymous mutations in mprF, of which 6 were novel mutations. Introduction of individual mprF mutation into a daptomycin-susceptible S. aureus strain led to DAP-R, resistance to CAMPs, and enhanced biosynthesis of L-PG. We confirmed that these mprF mutations were gain-of-function by expressing these mprF alleles in Escherichia coli and assessing the de novo biosynthesis of L-PG. To directly measure the impact of L-PG on daptomycin actions, we utilized the established bacterial membrane model coupled with high resolution neutron reflectometry.1 Increase of L-PG impaired daptomycin penetration and membrane solubilization despite of daptomycin association with the membranes. Replacement of L-PG with DOTAP reproduced this inhibition of daptomycin actions, indicating that increase of cationic charge was the mechanism behind mprF-mediated DAP-R. Interestingly, mutations in both mprF and cardiolipin synthase 2 (cls2) made MRSA hyper resistant to daptomycin, indicating that the L-PG mediated DAP-R mechanism is independent of a previously characterized mechanism by the enhanced cardiolipin biosynthesis.1 To disrupt this DAP-R mediated by MprF, we generated a loss-of-function mprF-D731A mutant, which disrupted the active site of L-PG synthesis as a proof of principle. This D731A mutation rendered the MRSA strain L-PG deficient and hypersusceptible to daptomycin, confirming the importance of L-PG in S. aureus. Together, our results illustrate that S. aureus is capable of utilizing diverse metabolic strategies to circumvent attacks from antibiotics and immune systems, providing important insights into membrane-targeting therapeutic strategies against this significant pathogen.