ArcB is a membrane-bound sensor histidine kinase. It is unusual in that it contains three distinct signaling domains. It senses oxygen levels in the cell by interacting with reduced quinone. When reduced quinone levels are high, it signals that the cell is engaged in aerobic respiration. When reduced quinone levels are low, it signals that the cells is unable to perform aerobic respiration. This is typically due to insufficient levels of oxygen, which acts as the terminal electron receptor in the electron transport chain. ArcB is then able to activate or deactivate ArcA, the response regulator, which can then travel to the chromosome and regulate gene expression.
ArcA is activated via phosphorylation. When oxygen is present in the cell ArcB autophosphorylates. This inorganic phosphate is then transferred via a four amino acid phosphorelay to ArcA. Phosphorylated ArcA is then able to attach to specific, consensus gene sequences on the chromosome regulating approximately 30 different operons. ArcA is able to acts as both a repressor and an activator depending on which operon it attaches.
When oxygen levels are low, ArcB acts as a phosphatase, removing the inorganic phosphate group from ArcA. Without the attached phosphate group, ArcA is unable to bind to DNA and genes return to their original, aerobic levels of expression. This allows the cell to engage in metabolic pathways that are most advantageous for the current conditons of the cell. Dephosphorylation utilizes the same phosphorelay as phosphorylation, but it is operated in reverse.
Without the Arc system being present throughout various strains of anaerobic bacteria, gene expression could not efficiently control the metabolism during the replication of genetic material. Under many growth conditions where oxygen is not present, the ArcB sensor kinase (which is membrane-bound) turns to autophosphorylates which is a process proven to be more efficient when certain fermenting metabolites such as Pyruvate, Acetate, and D-Lactate.