Protein Family Models

CheX is very closely related to the CheC chemotaxis phosphatase, but it dimerises in a different way, via a continuous beta sheet between the subunits. CheC and CheX both dephosphorylate CheY, although CheC requires binding of CheD to achieve the activity of CheX. The ability of bacteria to modulate their swimming behaviour in the presence of external chemicals (nutrients and repellents) is one of the most rudimentary behavioural responses known, but the the individual components are very sensitively tuned [1]. [1]. 15546616. Structure and function of an unusual family of protein phosphatases: the bacterial chemotaxis proteins CheC and CheX. Park SY, Chao X, Gonzalez-Bonet G, Beel BD, Bilwes AM, Crane BR;. Mol Cell. 2004;16:563-574. (from Pfam)

Date:

2024-10-16

The restoration of pre-stimulus levels of the chemotactic response regulator, CheY-P, is important for allowing bacteria to respond to new environmental stimuli. The members of this family, CheC, CheX, CheA and FliY are CheY-P phosphatase [1,2]. CheC appears to be primarily involved in restoring normal CheY-P levels, whereas FliY seems to act on CheY-P constitutively. CheD enhances the activity of CheC 5-fold, which is normally relatively low [1,2]. In some cases, the region represented by this entry is present as multiple copies. [1]. 14749334. Bacillus subtilis CheC and FliY are members of a novel class of CheY-P-hydrolyzing proteins in the chemotactic signal transduction cascade. Szurmant H, Muff TJ, Ordal GW;. J Biol Chem 2004;279:21787-21792. [2]. 15187186. Diversity in chemotaxis mechanisms among the bacteria and archaea. Szurmant H, Ordal GW;. Microbiol Mol Biol Rev 2004;68:301-319. (from Pfam)

Date:

2024-10-16

chemotaxis protein CheX dephosphorylates CheY to control levels of CheY-P

Date:

2020-02-25