Unlike in rod-shaped bacteria, cell polarity is not well defined in cocci and possibly getsmarked duringmolecular events around cytokinesis. DivIVA is amember ofMin systemthat is involved in spatial regulation of septumformation in bacteria. Recently, we showed that DivIVA of Deinococcus radiodurans (drDivIVA) interacts with proteins involved in cell division and genome segregation (segrosome). To map drDivIVA domain (s) that interact with these proteins, the N-terminal (DivIVA-N), C-terminal (DivIVA-C) and a middle (DivIVA-M) region/section of drDivIVA were generated. Circular Dichroism (CD) studies suggested that all three variants of drDivIVA fold properly, but they appeared different under transmission electron microscopy (TEM). Full length drDivIVA showed bundles under TEMwhereas variants did not. Both full length drDivIVA and N-terminal domain showed repeats of heptadmotifs, a characteristic of alpha-helical coiled-coil proteins. DivIVA-N showed dimerization and interactionwith segrosome while DivIVA-MinteractedwithMinC, a cell division regulatory protein. Further, the C-terminal region seems to be crucial for the structural and functional integrity of drDivIVA. These results suggested that drDivIVA dimerizes through its N-terminal domainwhile both segrosome andMinC interact through different regions of this protein.