{PDOC50851}
{PS50851; CHEW}
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* CheW-like domain profile *
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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 beta-sheet subdomains, each of which
forms a  loose  five-stranded  beta-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 beta-sheet subdomains. The
CheW-like structure is stabilized by extensive hydrophobic interactions [1,4].

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

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: January 2003 / First entry.

[ 1] Bilwes A.M., Alex L.A., Crane B.R., Simon M.I.
     "Structure of CheA, a signal-transducing histidine kinase."
     Cell 96:131-141(1999).
     PubMed=9989504
[ 2] Karatan E., Saulmon M.M., Bunn M.W., Ordal G.W.
     "Phosphorylation of the response regulator CheV is required for
     adaptation to attractants during Bacillus subtilis chemotaxis."
     J. Biol. Chem. 276:43618-43626(2001).
     PubMed=11553614; DOI=10.1074/jbc.M104955200
[ 3] Alexandre G., Zhulin I.B.
     "Different evolutionary constraints on chemotaxis proteins CheW and
     CheY revealed by heterologous expression studies and protein sequence
     analysis."
     J. Bacteriol. 185:544-552(2003).
     PubMed=12511501
[ 4] Griswold I.J., Zhou H., Matison M., Swanson R.V., McIntosh L.P.,
     Simon M.I., Dahlquist F.W.
     "The solution structure and interactions of CheW from Thermotoga
     maritima."
     Nat. Struct. Biol. 9:121-125(2002).
     PubMed=11799399; DOI=10.1038/nsb753

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