Worldwide, the alarming increase in multidrug resistance in bacterial strains such as Methicillin-resistant Staphylococcus aureus (MRSA), drug-resistant tuberculosis (NDM-1), vancomycin-resistant enterococci (VRE) and other bacteria has posed a serious threat to human health. Further, with no significant antibiotic development in the last few decades, there are few treatment options left to deal with infectious diseases, particularly in immunocompromised patients. Majority of clinically used antibacterial drugs target classical pathways of DNA, RNA, protein or cell wall biosynthesis. Considering the increasing prevalence of bacteria with reduced susceptibility to current antibiotics, there is an urgent need to discover new antibacterial agents with novel targets and mechanism of action. Bacterial cells are critically dependent on their ability to divide where cell division is carried out by a complex, highly dynamic molecular machine, known as the divisome. In recent years, bacterial cell division has drawn considerable interest among the scientific community and is seen as a promising target pathway for the discovery of novel antibacterials. Before the 1990s, it was not even known that cytoskeletons existed in prokaryotes. They were believed to be present only in eukaryotes. However, later in the 1990s, with development in advanced imaging techniques scientist conducted studies that showed the presence of cytoskeleton-like structures in several prokaryotes. The homologs of eukaryotic cytoskeletons, such as microtubules, microfilaments, and intermediate filaments, were identified in bacteria and archaea. More than a dozen proteins have been identified in bacterial cell division and most of them are essential for the growth of bacteria. Thus, any inhibition of activity or assembly of these proteins as part of the division machinery result in loss of viability and cell death in several bacterial species. Cell division in bacteria is a very highly regulated process and is guided by a ring-like structure, known as Z-ring, formed by filamentous temperature- sensitive protein, FtsZ. There are several proteins associated with the Z-ring formation. FtsZ is an important cell-division protein conserved in essentially all bacteria. It is the first protein to localize at the division site and is required through the final step of cell division. Basically, it forms a highly dynamic Z-ring at the center of the cell and then recruits other cell division proteins. After the completion of recruitment, the Z ring contracts, leading to the closure of the septum along with the formation of two identical daughter cells. Besides, serving as a scaffold for other cell division proteins, FtsZ exert cytokinetic forces that lead to cell division. Owing to its crucial role in cell division, FtsZ has generated a great deal of interests among researchers to develop a new generation of novel antibacterial agents. In recent years, a number of compounds have been reported that modulate the assembly/disassembly dynamics of FtsZ, some of which have shown promising antibacterial activity in in vitro and in vivo models of infection. Thus, FtsZ inhibitors have been looked upon as future candidate for new antimicrobials (broad-spectrum and pathogen-specific). So let’s join hand and be in the ring (FtsZ world) to fight the war against antibiotic drug resistance and explore cell division in bacteria as a novel target for developing newer antibacterials with us (ProCyto labs).