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PROSITE documentation PDOC50851 [for PROSITE entry PS50851]

CheW-like domain profile





Description

The CheW-like domain is an around 150-residue domain that is found in proteins involved in the two-component signaling systems regulating bacterial chemotaxis. Two components systems are composed of a receptor kinase, which monitors the environmental conditions and its substrate, the response regulator, which acts as a binary switch depending on the phosphorylation state. In Escherichia coli, the signal transduction pathway for chemotaxis consists of specialized membrane receptors, termed chemotaxis transducers; a CheA-CheY two-component system, which transmits the signal from transducers to flagellar motors; and a docking protein, CheW, which couples the CheA histidine kinase to transducers. Whereas CheW is only made of a CheW-like domain, CheA additionally contains an HPt domain (see <PDOC50894>) and an histidine kinase domain (see <PDOC50109>). The CheW-like domain has been shown to mediate the interaction between CheA and the adaptor protein CheW. Some bacteria contain another bifunctional protein, CheV, consisting of an N-terminal CheW-like domain and a C-terminal response regulatory domain (see <PDOC50110>). Although its precise function in chemotaxis is unknown, CheV probably acts in adaptation to attractants [1,2,3,4].

The CheW-like domain is composed of two β-sheet subdomains, each of which forms a loose five-stranded β-barrel around an internal hydrophobic core (see <PDB:1K0S>). The interactions between the subdomains are contributed by a third hydrophobic core sandwiched between the two β-sheet subdomains. The CheW-like structure is stabilized by extensive hydrophobic interactions [1,4].

The profile we developed covers the entire CheW-like domain.

Last update:

January 2003 / First entry.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

CHEW, PS50851; CheW-like domain profile  (MATRIX)


References

1AuthorsBilwes A.M. Alex L.A. Crane B.R. Simon M.I.
TitleStructure of CheA, a signal-transducing histidine kinase.
SourceCell 96:131-141(1999).
PubMed ID9989504

2AuthorsKaratan E. Saulmon M.M. Bunn M.W. Ordal G.W.
TitlePhosphorylation of the response regulator CheV is required for adaptation to attractants during Bacillus subtilis chemotaxis.
SourceJ. Biol. Chem. 276:43618-43626(2001).
PubMed ID11553614
DOI10.1074/jbc.M104955200

3AuthorsAlexandre G. Zhulin I.B.
TitleDifferent evolutionary constraints on chemotaxis proteins CheW and CheY revealed by heterologous expression studies and protein sequence analysis.
SourceJ. Bacteriol. 185:544-552(2003).
PubMed ID12511501

4AuthorsGriswold I.J. Zhou H. Matison M. Swanson R.V. McIntosh L.P. Simon M.I. Dahlquist F.W.
TitleThe solution structure and interactions of CheW from Thermotoga maritima.
SourceNat. Struct. Biol. 9:121-125(2002).
PubMed ID11799399
DOI10.1038/nsb753



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