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<i>Background:</i> Prolactin inducible protein (PIP) is a small secretary glycoprotein present in most biological fluids and contributes to various cellular functions, including cell growth, fertility, antitumor, and antifungal activities. <i>Objectives:</i> The present study evaluated the antibacterial activities of recombinant PIP against multiple broad-spectrum MDR bacterial strains. <i>Methods:</i> The PIP gene was cloned, expressed and purified using affinity chromatography. Disk diffusion, broth microdilution, and growth kinetic assays were used to determine the antibacterial activities of PIP. <i>Results</i>: Disk diffusion assay showed that PIP has a minimum and maximum zone of inhibition against <i>E. coli</i> and <i>P. aeruginosa</i>, respectively, compared to the reference drug ampicillin. Furthermore, growth kinetics studies also suggested that PIP significantly inhibited the growth of <i>E. coli</i> and <i>P. aeruginosa</i>. The minimum inhibitory concentration of PIP was 32 µg/mL for <i>E. coli</i> (443), a standard bacterial strain, and 64 µg/mL for <i>Bacillus</i> sp. (LG1), an environmental multidrug-resistant (MDR) strain. The synergistic studies of PIP with ampicillin showed better efficacies towards selected bacterial strains having MDR properties. <i>Conclusion:</i> Our findings suggest that PIP has a broad range of antibacterial activities with important implications in alleviating MDR problems.