CHEW_ECOLI
ID CHEW_ECOLI Reviewed; 167 AA.
AC P0A964; P07365;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Chemotaxis protein CheW;
GN Name=cheW; OrderedLocusNames=b1887, JW1876;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3510184; DOI=10.1128/jb.165.1.161-166.1986;
RA Mutoh N., Simon M.I.;
RT "Nucleotide sequence corresponding to five chemotaxis genes in Escherichia
RT coli.";
RL J. Bacteriol. 165:161-166(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32.
RX PubMed=2002011; DOI=10.1128/jb.173.6.2116-2119.1991;
RA Kofoid E.C., Parkinson J.S.;
RT "Tandem translation starts in the cheA locus of Escherichia coli.";
RL J. Bacteriol. 173:2116-2119(1991).
RN [6]
RP SUBUNIT.
RX PubMed=2068106; DOI=10.1073/pnas.88.14.6269;
RA McNally D.F., Matsumura P.;
RT "Bacterial chemotaxis signaling complexes: formation of a CheA/CheW complex
RT enhances autophosphorylation and affinity for CheY.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:6269-6273(1991).
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.
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. {ECO:0000269|PubMed:2068106}.
CC -!- INTERACTION:
CC P0A964; P07017: tar; NbExp=5; IntAct=EBI-1125947, EBI-1125130;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
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DR EMBL; M13462; AAA23565.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74957.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15703.1; -; Genomic_DNA.
DR EMBL; M34669; AAA23575.1; -; Genomic_DNA.
DR PIR; B25195; QRECCW.
DR RefSeq; NP_416401.1; NC_000913.3.
DR RefSeq; WP_000147302.1; NZ_STEB01000026.1.
DR PDB; 2HO9; NMR; -; A=1-167.
DR PDB; 6S1K; EM; 8.38 A; C/D=1-167.
DR PDBsum; 2HO9; -.
DR PDBsum; 6S1K; -.
DR AlphaFoldDB; P0A964; -.
DR BMRB; P0A964; -.
DR SMR; P0A964; -.
DR BioGRID; 4261038; 235.
DR BioGRID; 850757; 2.
DR DIP; DIP-48236N; -.
DR IntAct; P0A964; 31.
DR STRING; 511145.b1887; -.
DR PaxDb; P0A964; -.
DR PRIDE; P0A964; -.
DR EnsemblBacteria; AAC74957; AAC74957; b1887.
DR EnsemblBacteria; BAA15703; BAA15703; BAA15703.
DR GeneID; 66674222; -.
DR GeneID; 946400; -.
DR KEGG; ecj:JW1876; -.
DR KEGG; eco:b1887; -.
DR PATRIC; fig|1411691.4.peg.360; -.
DR EchoBASE; EB0147; -.
DR eggNOG; COG0835; Bacteria.
DR HOGENOM; CLU_048995_1_0_6; -.
DR InParanoid; P0A964; -.
DR OMA; CVNIMSV; -.
DR PhylomeDB; P0A964; -.
DR BioCyc; EcoCyc:CHEW-MON; -.
DR EvolutionaryTrace; P0A964; -.
DR PHI-base; PHI:6536; -.
DR PRO; PR:P0A964; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0051286; C:cell tip; IDA:CACAO.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0098561; C:methyl accepting chemotaxis protein complex; IDA:CAFA.
DR GO; GO:0005886; C:plasma membrane; IDA:CAFA.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0009454; P:aerotaxis; IDA:EcoCyc.
DR GO; GO:0006935; P:chemotaxis; IMP:EcoCyc.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:CACAO.
DR GO; GO:1901875; P:positive regulation of post-translational protein modification; IDA:CAFA.
DR GO; GO:0010864; P:positive regulation of protein histidine kinase activity; IDA:EcoCyc.
DR GO; GO:0007165; P:signal transduction; IDA:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Chemotaxis; Cytoplasm; Reference proteome.
FT CHAIN 1..167
FT /note="Chemotaxis protein CheW"
FT /id="PRO_0000198341"
FT DOMAIN 16..156
FT /note="CheW-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00052"
FT CONFLICT 16
FT /note="G -> R (in Ref. 5; AAA23575)"
FT /evidence="ECO:0000305"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:2HO9"
FT STRAND 17..24
FT /evidence="ECO:0007829|PDB:2HO9"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:2HO9"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:2HO9"
FT STRAND 36..42
FT /evidence="ECO:0007829|PDB:2HO9"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:2HO9"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:2HO9"
FT HELIX 71..75
FT /evidence="ECO:0007829|PDB:2HO9"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:2HO9"
FT STRAND 96..111
FT /evidence="ECO:0007829|PDB:2HO9"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:2HO9"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:2HO9"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:2HO9"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:2HO9"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:2HO9"
FT HELIX 147..158
FT /evidence="ECO:0007829|PDB:2HO9"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:2HO9"
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
