The diverse CheC-type phosphatases: Chemotaxis and beyond

Travis J. Muff, George W. Ordal

Research output: Contribution to journalShort survey

Abstract

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-X3-E-X2-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.

Original languageEnglish (US)
Pages (from-to)1054-1061
Number of pages8
JournalMolecular Microbiology
Volume70
Issue number5
DOIs
StatePublished - Dec 1 2008

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

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