Moreover, an entire group of phospholipid synthases localizes to the division septum of B. One of these is the chaperonin GroEL, which may function in folding cell division proteins, but clearly folds many proteins in the cell. The division site at midcell also attracts other proteins that are not obviously connected with cell division but which require FtsZ for proper localization there. In most cases, the localization of these proteins depends upon FtsZ, indicating that they are recruited by the Z ring.Ī Also localizes to cell poles in rod-shaped bacteria. subtilis YlmF (which can substitute for FtsA), FtsE (which interacts with FtsX), ZapB, ZapC and ZapD. Other cytoplasmic proteins that localize at the division site include B. FtsX is a nonessential polytopic division protein that localizes to the Z ring. Other periplasmic proteins associated with the division site include the cell wall amidases EnvC and AmiC and the Tol/Pal complex. The precise activities of these proteins are unknown, with the exception of FtsI, which is a septal transpeptidase and also called PBP3. Many of these proteins have conserved orthologues in other species, although FtsN is only found in close relatives of E.
coli include the polytopic proteins FtsK and FtsW and bitopic proteins FtsB, FtsQ, FtsL, FtsI, and FtsN. The transmembrane division proteins essential for cell division in E. However, a large number of other proteins localize to the division site, and most of them have some function in cell division ( Table 2). Several components of the cell division apparatus, including FtsZ, FtsA, ZipA, and ZapA, were discussed earlier.