CHEW_ECO57
ID CHEW_ECO57 Reviewed; 167 AA.
AC P0A966; P07365;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Chemotaxis protein CheW;
GN Name=cheW; OrderedLocusNames=Z2941, ECs2597;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG56877.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB36020.1; -; Genomic_DNA.
DR PIR; E90953; E90953.
DR RefSeq; NP_310624.1; NC_002695.1.
DR RefSeq; WP_000147302.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0A966; -.
DR BMRB; P0A966; -.
DR SMR; P0A966; -.
DR STRING; 155864.EDL933_2862; -.
DR EnsemblBacteria; AAG56877; AAG56877; Z2941.
DR EnsemblBacteria; BAB36020; BAB36020; ECs_2597.
DR GeneID; 66674222; -.
DR GeneID; 914106; -.
DR KEGG; ece:Z2941; -.
DR KEGG; ecs:ECs_2597; -.
DR PATRIC; fig|386585.9.peg.2723; -.
DR eggNOG; COG0835; Bacteria.
DR HOGENOM; CLU_048995_1_0_6; -.
DR OMA; CVNIMSV; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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; Reference proteome.
FT CHAIN 1..167
FT /note="Chemotaxis protein CheW"
FT /id="PRO_0000198342"
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