Histidine kinase involved in a two-component signaling pathway that regulates cell wall mannan and glucan biosynthesis. Regulates quorum sensing as well as hyphal formation, biofilm formation, chlamidospore formation, and virulence. Plays a prominent role in phagocyte activation. Involved in the covering of the most potent pro-inflammatory cell wall molecules, the beta-glucans, underneath a dense mannan layer, so that the pathogen becomes partly invisible for immune cells such as phagocytes. ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. Expression is detected as early as 1 hour after infection of reconstituted human esophageal tissue and increases thereafter up to 48 hours postinfection. Expression is also increased when cells are exposed to several types of stress. Expression is decreased by Pseudomonas aeruginosa secretions. Moreover, expression is regulated by NGR1 and BCR1. The protein kinase domain is predicted to be catalytically inactive. The phosphorelay mechanism involves the sequential transfer of a phosphate group from His-2007 (H1) in the histidine kinase domain (transmitter domain) to Asp-2394 (D1) of the response regulatory domain (receiver domain). This transfer probably occurs between two CHK1 molecules, rather than intramolecularly (By similarity). Impairs the hyphal formation and attenuates the virulence in a mouse systemic candidiasis model and towards reconstituted human esophageal tissue. Leads to extensive flocculation under conditions that stimulate germ-tube formation. Leads also to increased growth-inhibitory and killing effect by human neutrophils (polymorphonuclear leukocytes) and to hypersensitivity to fluconazole and voriconazole.