PMID:12920116

Citation	Szurmant, H, Bunn, MW, Cannistraro, VJ and Ordal, GW (2003) Bacillus subtilis hydrolyzes CheY-P at the location of its action, the flagellar switch. J. Biol. Chem. 278:48611-6
Abstract	In this report we show that in Bacillus subtilis the flagellar switch, which controls direction of flagellar rotation based on levels of the chemotaxis primary response regulator, CheY-P, also causes hydrolysis of CheY-P to form CheY and Pi. This task is performed in Escherichia coli by CheZ, which interestingly enough is primarily located at the receptors, not at the switch. In particular we have identified the phosphatase as FliY, which resembles E. coli switch protein FliN only in its C-terminal part, while an additional N-terminal domain is homologous to another switch protein FliM and to CheC, a protein found in the archaea and many bacteria but not in E. coli. Previous E. coli studies have localized the CheY-P binding site of the switch to FliM residues 6-15. These residues are almost identical to the residues 6-15 in both B. subtilis FliM and FliY. We were able to show that both of these proteins are capable of binding CheY-P in vitro. Deletion of this binding region in B. subtilis mutant fliM caused the same phenotype as a cheY mutant (clockwise flagellar rotation), whereas deletion of it in fliY caused the opposite. We showed that FliY increases the rate of CheY-P hydrolysis in vitro. Consequently, we imagine that the duration of enhanced CheY-P levels caused by activation of the CheA kinase upon attractant binding to receptors, is brief due both to adaptational processes and to phosphatase activity of FliY.
Links	PubMed Online version:10.1074/jbc.M306180200
Keywords	Amino Acid Sequence; Bacillus subtilis/metabolism; Bacillus subtilis/physiology; Bacterial Proteins; Binding Sites; Chemotaxis; Hydrolysis; Membrane Proteins/chemistry; Membrane Proteins/metabolism; Molecular Sequence Data; Phosphorylation; Recombinant Fusion Proteins/metabolism; Sequence Homology, Amino Acid
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
BACSU:FLIY	involved_in	GO:0006935: chemotaxis	ECO:0000315: mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
BACSU:FLIY	enables	GO:0004721: phosphoprotein phosphatase activity	ECO:0000314: direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
BACSU:FLIY	involved_in	GO:0016311: dephosphorylation	ECO:0000315: mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
BACSU:FLIY		GO:0004721: phosphoprotein phosphatase activity	ECO:0000314:		F		Figure 5 shows Fliy activity in dephosphorylation of Chey-P	complete CACAO 2133
BACSU:FLIY	involved_in	GO:1902021: regulation of bacterial-type flagellum-dependent cell motility	ECO:0000315: mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
BACSU:FLIY		GO:0006935: chemotaxis	ECO:0000315:		P		See Figure 4 and Results: N-terminal Deletions in FliM and FliY Promote Opposite Phenotypes in the Tethered Cell Assay in Vivo. FliY mutant did not match wild-type swarm diameters and did not respond to addition or removal of the attractant asparagine.	complete CACAO 10481
BACSU:FLIY		GO:1902021: regulation of bacterial-type flagellum-dependent cell motility	ECO:0000315:		P		"See Results: N-terminal Deletions in FliM and FliY Promote Opposite Phenotypes in the Tethered Cell Assay in Vivo. Figure 4B shows that the modified FliY causes rotational direction of a tethered cell to reverse in a tethered cell assay.	complete CACAO 10484
BACSU:FLIY		GO:0016311: dephosphorylation	ECO:0000315:		P		See Fig 5: increasing concentrations of FliY increase the speed of CheY-P dephosphorylation.	complete
BACSU:FLIM		GO:0050918: positive chemotaxis	ECO:0000315:		P		See Figure 4 and Results: N-terminal Deletions in FliM and FliY Promote Opposite Phenotypes in the Tethered Cell Assay in Vivo. FliM mutant did not match wild-type swarm diameters and did not respond to addition or removal of the attractant asparagine.	complete CACAO 10485
BACSU:FLIM	involved_in	GO:0050918: positive chemotaxis	ECO:0000315: mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete

References

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