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The diverse CheC‐type phosphatases: chemotaxis and beyond
Author(s) -
Muff Travis J.,
Ordal George W.
Publication year - 2008
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2008.06482.x
Subject(s) - chemotaxis , phosphatase , biology , bacillus subtilis , function (biology) , class (philosophy) , sequence (biology) , dimer , phosphorylation , genetics , bacteria , chemistry , receptor , artificial intelligence , computer science , organic chemistry
Summary A new class of protein phosphatases has emerged in the study of bacterial/archaeal chemotaxis, the CheC‐type phosphatases. These proteins are distinct and unrelated to the well‐known CheY‐P phosphatase CheZ, though they have convergently evolved to dephosphorylate the same target. The family contains a common consensus sequence D/S‐X 3 ‐E‐X 2 ‐N‐X 22 ‐P that defines the phosphatase active site, of which there are often two per protein. Three distinct subgroups make up the family: CheC, FliY and CheX. Further, the CheC subgroup can be divided into three classes. Bacillus subtilis CheC typifies the first class and might function as a regulator of CheD. Class II CheCs likely function as phosphatases in systems other than chemotaxis. Class III CheCs are found in the archaeal class Halobacteria and might function as class I CheCs. FliY is the main phosphatase in the B. subtilis chemotaxis system. CheX is quite divergent from the rest of the family, forms a dimer and some may function outside chemotaxis. A model for the evolution of the family is discussed.