CHEW_SHIFL
ID CHEW_SHIFL Reviewed; 167 AA.
AC P0A967; P07365;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Chemotaxis protein CheW;
GN Name=cheW; OrderedLocusNames=SF1936, S2027;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN43489.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP17319.1; -; Genomic_DNA.
DR RefSeq; NP_707782.1; NC_004337.2.
DR RefSeq; WP_000147302.1; NZ_WPGW01000105.1.
DR AlphaFoldDB; P0A967; -.
DR BMRB; P0A967; -.
DR SMR; P0A967; -.
DR STRING; 198214.SF1936; -.
DR EnsemblBacteria; AAN43489; AAN43489; SF1936.
DR EnsemblBacteria; AAP17319; AAP17319; S2027.
DR GeneID; 1023709; -.
DR GeneID; 66674222; -.
DR KEGG; sfl:SF1936; -.
DR KEGG; sfx:S2027; -.
DR PATRIC; fig|198214.7.peg.2311; -.
DR HOGENOM; CLU_048995_1_0_6; -.
DR OMA; CVNIMSV; -.
DR OrthoDB; 1711729at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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_0000198348"
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
