Macromolecular structures such as the bacterial flagellum in Gram-negative bacteria must traverse the cell wall. Lytic transglycosylases are capable of enlarging gaps in the peptidoglycan meshwork to allow the efficient assembly of supramolecular complexes. We have previously shown that in Rhodobacter sphaeroides SltF, the flagellar muramidase, and FlgJ, a flagellar scaffold protein, are separate entities that interact in the periplasm. In this study we show that the export of SltF to the periplasm is dependent on the SecA pathway. A deletion analysis of the C-terminal portion of SltF shows that this region is required for SltF-SltF interaction. These C terminus-truncated mutants lose the capacity to interact with themselves and also bind FlgJ with higher affinity than does the wild-type protein. We propose that this region modulates the interaction with the scaffold protein FlgJ during the assembly process.