It has long been known that many proteins are capable of liquid-liquid phase separation (LLPS), in which protein droplets separate from the surrounding aqueous phase. The overall biological significance of this phenomenon has only received greater attention lately, being important in several complex biological processes. Moreover, LLPS appears to be an efficient method for compartmentalization, which is even more pronounced in case of lower organisms like bacteria, as they do not possess internal membrane systems for spatial separation. The E. coli single-stranded DNA binding protein (EcSSB) was recently shown by our group to be able to form LLPS, and it was suggested that this ability might confers significant adaptive advantages to bacterial cells. If this proves to be the case during our research, it will raise the possibility that LLPS and/or SSBs and their interaction network will be suitable for subcellular targeting by antibacterial drugs. This possibility is supported by the fact that similar proteins in higher organisms (such as humans) exhibit a phase separation propensity that is very different from that of bacterial proteins. Moreover, phase-separated condensates contain high concentrations of protein and can be easily separated from the surrounding aqueous phase, opening the possibility for technological exploitation in the production and purification of various macromolecules.