ID   CHEW_ECOL6              Reviewed;         167 AA.
AC   P0A965; P07365;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Chemotaxis protein CheW;
GN   Name=cheW; OrderedLocusNames=c2302;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Involved in the transmission of sensory signals from the
CC       chemoreceptors to the flagellar motors. It physically bridges CheA to
CC       the MCPs (methyl-accepting chemotaxis proteins) to allow regulated
CC       phosphotransfer to CheY and CheB (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: An in vitro complex of CheW/CheA(L)/CheA(S) in a 1:1:1 ratio
CC       increases the autophosphorylation of CheA and is required for the
CC       binding of CheY, the phosphorylation substrate. This complex accounts
CC       for 10% of the total number of molecules (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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DR   EMBL; AE014075; AAN80761.1; -; Genomic_DNA.
DR   RefSeq; WP_000147302.1; NC_004431.1.
DR   AlphaFoldDB; P0A965; -.
DR   BMRB; P0A965; -.
DR   SMR; P0A965; -.
DR   STRING; 199310.c2302; -.
DR   EnsemblBacteria; AAN80761; AAN80761; c2302.
DR   GeneID; 66674222; -.
DR   KEGG; ecc:c2302; -.
DR   eggNOG; COG0835; Bacteria.
DR   HOGENOM; CLU_048995_1_0_6; -.
DR   OMA; CVNIMSV; -.
DR   BioCyc; ECOL199310:C2302-MON; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR039315; CheW.
DR   InterPro; IPR036061; CheW-like_dom_sf.
DR   InterPro; IPR002545; CheW-lke_dom.
DR   PANTHER; PTHR22617; PTHR22617; 1.
DR   Pfam; PF01584; CheW; 1.
DR   SMART; SM00260; CheW; 1.
DR   SUPFAM; SSF50341; SSF50341; 1.
DR   PROSITE; PS50851; CHEW; 1.
PE   3: Inferred from homology;
KW   Chemotaxis; Cytoplasm.
FT   CHAIN           1..167
FT                   /note="Chemotaxis protein CheW"
FT                   /id="PRO_0000198343"
FT   DOMAIN          16..156
FT                   /note="CheW-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00052"
SQ   SEQUENCE   167 AA;  18084 MW;  9CE642E5F4E91BFF CRC64;
     MTGMTNVTKL ASEPSGQEFL VFTLGDEEYG IDILKVQEIR GYDQVTRIAN TPAFIKGVTN
     LRGVIVPIVD LRIKFSQVDV DYNDNTVVIV LNLGQRVVGI VVDGVSDVLS LTAEQIRPAP
     EFAVTLSTEY LTGLGALGDR MLILVNIEKL LNSEEMALLD SAASEVA