DgrA/B

The concentration of c-di-GMP is varying, and for our experiment we will promote its expression to inhibit rotation of flagella. It will bind to DgrA and DgrB. The resulting complex will have two routes to go: one is the [c-di-GMP&DgrA] complex which will inhibit FliL, a protein bound to the membrane playing a key role in rotation of flagella. And the other route is that the DgrB will directly affect the rotation of the flagella.

HfiA/HfsJ

Ref: A Cell Cycle and Nutritional Checkpoint Controlling Bacterial Surface Adhesion

In this paper, author describes a novel regulatory mechanism by which the C.c. bacterium integrates cell cycle and nutritional signals to control development of an adhesive envelop structure known as holdfast.

They discovered a novel inhibitor of holdfast development. HfiA, that is regulated downstream of lovK-lovR. They also discovered a bio-synthesis related gene named HfsJ. And the suppressing mutations in HfsJ attenuate the HfsJ-HfiA interaction.

These results support a model in which HfiA inhibits holdfast development via direct interaction with an enzyme required for holdfast biosynthesis

In conclusion, author says: We demonstrate that the predicted glycosyltransferase, HfsJ, is a required component of the holdfast development machinery and that residues at the C-terminus of HsfJ mediate a direct interaction with HfiA, leading to a post-translational inhibition of HfsJ.