CHEY_ECOLI
ID CHEY_ECOLI Reviewed; 129 AA.
AC P0AE67; P06143;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Chemotaxis protein CheY;
GN Name=cheY; OrderedLocusNames=b1882, JW1871;
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=6090423; DOI=10.1128/jb.160.1.36-41.1984;
RA Matsumura P., Rydel J.J., Linzmeier R., Vacante D.;
RT "Overexpression and sequence of the Escherichia coli cheY gene and
RT biochemical activities of the CheY protein.";
RL J. Bacteriol. 160:36-41(1984).
RN [2]
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 [3]
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 [4]
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 [5]
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 [6]
RP PHOSPHORYLATION.
RX PubMed=3280143; DOI=10.1016/0092-8674(88)90489-8;
RA Hess J.F., Oosawa K., Kaplan N., Simon M.I.;
RT "Phosphorylation of three proteins in the signaling pathway of bacterial
RT chemotaxis.";
RL Cell 53:79-87(1988).
RN [7]
RP PHOSPHORYLATION AT ASP-57, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2689446; DOI=10.1016/s0021-9258(20)88250-7;
RA Sanders D.A., Gillece-Castro B.L., Stock A.M., Burlingame A.L.,
RA Koshland D.E. Jr.;
RT "Identification of the site of phosphorylation of the chemotaxis response
RT regulator protein, CheY.";
RL J. Biol. Chem. 264:21770-21778(1989).
RN [8]
RP ACETYLATION AT LYS-109.
RX PubMed=1390767; DOI=10.1021/bi00156a033;
RA Barak R., Welch M., Yanovsky A., Oosawa K., Eisenbach M.;
RT "Acetyladenylate or its derivative acetylates the chemotaxis protein CheY
RT in vitro and increases its activity at the flagellar switch.";
RL Biochemistry 31:10099-10107(1992).
RN [9]
RP DEPHOSPHORYLATION BY CHEAS/CHEZ COMPLEX.
RX PubMed=8820640; DOI=10.1046/j.1365-2958.1996.393934.x;
RA Wang H., Matsumura P.;
RT "Characterization of the CheAS/CheZ complex: a specific interaction
RT resulting in enhanced dephosphorylating activity on CheY-phosphate.";
RL Mol. Microbiol. 19:695-703(1996).
RN [10]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [11]
RP ACETYLATION AT LYS-92 AND LYS-109 BY ACETYL-COA SYNTHETASE, MASS
RP SPECTROMETRY, AND MUTAGENESIS OF LYS-92.
RX PubMed=9560203; DOI=10.1073/pnas.95.9.4918;
RA Ramakrishnan R., Schuster M., Bourret R.B.;
RT "Acetylation at Lys-92 enhances signaling by the chemotaxis response
RT regulator protein CheY.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:4918-4923(1998).
RN [12]
RP ACETYLATION AT LYS-92.
RX PubMed=11359578; DOI=10.1046/j.1365-2958.2001.02425.x;
RA Barak R., Eisenbach M.;
RT "Acetylation of the response regulator, CheY, is involved in bacterial
RT chemotaxis.";
RL Mol. Microbiol. 40:731-743(2001).
RN [13]
RP DEPHOSPHORYLATION BY CHEZ.
RX PubMed=17998207; DOI=10.1074/jbc.m704400200;
RA Silversmith R.E., Levin M.D., Schilling E., Bourret R.B.;
RT "Kinetic characterization of catalysis by the chemotaxis phosphatase CheZ.
RT Modulation of activity by the phosphorylated CheY substrate.";
RL J. Biol. Chem. 283:756-765(2008).
RN [14]
RP FUNCTION.
RC STRAIN=K12 / RP3098;
RX PubMed=20346719; DOI=10.1016/j.molcel.2010.03.001;
RA Paul K., Nieto V., Carlquist W.C., Blair D.F., Harshey R.M.;
RT "The c-di-GMP binding protein YcgR controls flagellar motor direction and
RT speed to affect chemotaxis by a 'backstop brake' mechanism.";
RL Mol. Cell 38:128-139(2010).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX PubMed=1869568; DOI=10.2210/pdb3chy/pdb;
RA Volz K., Matsumura P.;
RT "Crystal structure of Escherichia coli CheY refined at 1.7-A resolution.";
RL J. Biol. Chem. 266:15511-15519(1991).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS).
RX PubMed=8176739; DOI=10.1006/jmbi.1994.1308;
RA Bellsolell L., Prieto J., Serrano L., Coll M.;
RT "Magnesium binding to the bacterial chemotaxis protein CheY results in
RT large conformational changes involving its functional surface.";
RL J. Mol. Biol. 238:489-495(1994).
RN [17]
RP ERRATUM OF PUBMED:8176739.
RA Bellsolell L., Prieto J., Serrano L., Coll M.;
RL J. Mol. Biol. 242:103-103(1994).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANTS GLY-17 AND
RP GLY-14/GLY-15/GLY-17.
RX PubMed=8632450; DOI=10.1006/jmbi.1996.0151;
RA Bellsolell L., Cronet P., Majolero M., Serrano L., Coll M.;
RT "The three-dimensional structure of two mutants of the signal transduction
RT protein CheY suggest its molecular activation mechanism.";
RL J. Mol. Biol. 257:116-128(1996).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANTS TRP-106 AND
RP ILE-87/TRP-106.
RX PubMed=9030562; DOI=10.1074/jbc.272.8.5000;
RA Zhu X., Rebello J., Matsumura P., Volz K.;
RT "Crystal structures of CheY mutants Y106W and T87I/Y106W. CheY activation
RT correlates with movement of residue 106.";
RL J. Biol. Chem. 272:5000-5006(1997).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=9761905; DOI=10.1107/s0907444997012158;
RA Wilcock D., Pisabarro M.T., Lopez-Hernandez E., Serrano L., Coll M.;
RT "Structure analysis of two CheY mutants: importance of the hydrogen-bond
RT contribution to protein stability.";
RL Acta Crystallogr. D 54:378-385(1998).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH CHEA.
RX PubMed=9437425; DOI=10.1038/nsb0198-25;
RA Welch M., Chinardet N., Mourey L., Birck C., Samama J.-P.;
RT "Structure of the CheY-binding domain of histidine kinase CheA in complex
RT with CheY.";
RL Nat. Struct. Biol. 5:25-29(1998).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=9636149; DOI=10.1073/pnas.95.13.7333;
RA McEvoy M.M., Hausrath A.C., Randolph G.B., Remington S.J., Dahlquist F.W.;
RT "Two binding modes reveal flexibility in kinase/response regulator
RT interactions in the bacterial chemotaxis pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:7333-7338(1998).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANT VAL-95.
RX PubMed=10748173; DOI=10.1074/jbc.m909908199;
RA Schuster M., Zhao R., Bourret R.B., Collins E.J.;
RT "Correlated switch binding and signaling in bacterial chemotaxis.";
RL J. Biol. Chem. 275:19752-19758(2000).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF COMPLEX WITH ARCB.
RX PubMed=9761838; DOI=10.1107/s0907444997007075;
RA Kato M., Mizuno T., Hakoshima T.;
RT "Crystallization of a complex between a novel C-terminal transmitter, HPt
RT domain, of the anaerobic sensor kinase ArcB and the chemotaxis response
RT regulator CheY.";
RL Acta Crystallogr. D 54:140-142(1998).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), AND MUTAGENESIS OF ASP-12; ASP-13
RP AND ASP-57.
RX PubMed=11023787; DOI=10.1006/jmbi.2000.4507;
RA Sola M., Lopez-Hernandez E., Cronet P., Lacroix E., Serrano L., Coll M.,
RA Parraga A.;
RT "Towards understanding a molecular switch mechanism: thermodynamic and
RT crystallographic studies of the signal transduction protein CheY.";
RL J. Mol. Biol. 303:213-225(2000).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH CHEZ.
RX PubMed=12080332; DOI=10.1038/nsb816;
RA Zhao R., Collins E.J., Bourret R.B., Silversmith R.E.;
RT "Structure and catalytic mechanism of the E. coli chemotaxis phosphatase
RT CheZ.";
RL Nat. Struct. Biol. 9:570-575(2002).
RN [27]
RP STRUCTURE BY NMR.
RX PubMed=8354264; DOI=10.1111/j.1432-1033.1993.tb18068.x;
RA Bruix M., Pascual J., Santoro J., Prieto J., Serrano L., Rico M.;
RT "1H- and 15N-NMR assignment and solution structure of the chemotactic
RT Escherichia coli Che Y protein.";
RL Eur. J. Biochem. 215:573-585(1993).
RN [28]
RP STRUCTURE BY NMR.
RX PubMed=10731410; DOI=10.1006/jmbi.2000.3595;
RA Cho H.S., Lee S.-Y., Yan D., Pan X., Parkinson J.S., Kustu S., Wemmer D.E.,
RA Pelton J.G.;
RT "NMR structure of activated CheY.";
RL J. Mol. Biol. 297:543-551(2000).
CC -!- FUNCTION: Involved in the transmission of sensory signals from the
CC chemoreceptors to the flagellar motors. In its active (phosphorylated
CC or acetylated) form, CheY exhibits enhanced binding to a switch
CC component, FliM, at the flagellar motor which induces a change from
CC counterclockwise to clockwise flagellar rotation. Overexpression of
CC CheY in association with MotA and MotB improves motility of a ycgR
CC disruption, suggesting there is an interaction (direct or indirect)
CC between the c-di-GMP-binding flagellar brake protein and the flagellar
CC stator. {ECO:0000269|PubMed:20346719}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Note=Binds 1 Mg(2+) ion per subunit.;
CC -!- SUBUNIT: Interacts (phosphorylated CheY) with CheZ (via C-terminus).
CC {ECO:0000269|PubMed:12080332, ECO:0000269|PubMed:9437425}.
CC -!- INTERACTION:
CC P0AE67; P07363: cheA; NbExp=7; IntAct=EBI-546693, EBI-1026773;
CC P0AE67; P0A9H9: cheZ; NbExp=6; IntAct=EBI-546693, EBI-546726;
CC P0AE67; Q8KLS0: cheA3; Xeno; NbExp=2; IntAct=EBI-546693, EBI-15742036;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- PTM: Phosphorylated by CheA or acetylated by acetyl-CoA synthetase,
CC depending on which acetate metabolism pathway is available. The major
CC acetylation site seems to be Lys-92. Dephosphorylated (inactivated) by
CC CheZ. {ECO:0000269|PubMed:11359578, ECO:0000269|PubMed:1390767,
CC ECO:0000269|PubMed:2689446, ECO:0000269|PubMed:3280143,
CC ECO:0000269|PubMed:9560203}.
CC -!- MASS SPECTROMETRY: Mass=13966; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:9560203};
CC -!- MASS SPECTROMETRY: Mass=14008; Method=Electrospray; Note=With N6-
CC acetyl-Lys-92.; Evidence={ECO:0000269|PubMed:9560203};
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DR EMBL; K02175; AAA23577.1; -; Genomic_DNA.
DR EMBL; M13463; AAA23570.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74952.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15698.1; -; Genomic_DNA.
DR PIR; E25195; QRECCY.
DR RefSeq; NP_416396.1; NC_000913.3.
DR RefSeq; WP_000763867.1; NZ_STEB01000026.1.
DR PDB; 1A0O; X-ray; 2.95 A; A/C/E/G=2-129.
DR PDB; 1AB5; X-ray; 2.40 A; A/B=5-129.
DR PDB; 1AB6; X-ray; 2.20 A; A/B=5-129.
DR PDB; 1BDJ; X-ray; 2.68 A; A=2-129.
DR PDB; 1C4W; X-ray; 1.84 A; A=2-129.
DR PDB; 1CEY; NMR; -; A=2-129.
DR PDB; 1CHN; X-ray; 1.76 A; A=2-129.
DR PDB; 1CYE; NMR; -; A=3-129.
DR PDB; 1D4Z; X-ray; 1.90 A; A=2-129.
DR PDB; 1DJM; NMR; -; A=1-129.
DR PDB; 1E6K; X-ray; 2.00 A; A=3-129.
DR PDB; 1E6L; X-ray; 1.90 A; A=3-129.
DR PDB; 1E6M; X-ray; 1.70 A; A=3-129.
DR PDB; 1EAY; X-ray; 2.00 A; A/B=2-129.
DR PDB; 1EHC; X-ray; 2.26 A; A=2-129.
DR PDB; 1F4V; X-ray; 2.22 A; A/B/C=2-129.
DR PDB; 1FFG; X-ray; 2.10 A; A/C=2-129.
DR PDB; 1FFS; X-ray; 2.40 A; A/C=2-129.
DR PDB; 1FFW; X-ray; 2.70 A; A/C=2-129.
DR PDB; 1FQW; X-ray; 2.37 A; A/B=2-129.
DR PDB; 1HEY; X-ray; 2.24 A; A=2-129.
DR PDB; 1JBE; X-ray; 1.08 A; A=2-129.
DR PDB; 1KMI; X-ray; 2.90 A; Y=1-129.
DR PDB; 1MIH; X-ray; 2.70 A; A/B=1-129.
DR PDB; 1U8T; X-ray; 1.50 A; A/B/C/D=2-129.
DR PDB; 1UDR; X-ray; 1.90 A; A/B/C/D=1-129.
DR PDB; 1VLZ; X-ray; 2.05 A; A/B=2-129.
DR PDB; 1YMU; X-ray; 2.30 A; A/B=3-129.
DR PDB; 1YMV; X-ray; 1.90 A; A=3-129.
DR PDB; 1ZDM; X-ray; 2.40 A; A/B=1-129.
DR PDB; 2B1J; X-ray; 2.40 A; A/B=2-129.
DR PDB; 2ID7; X-ray; 1.75 A; A=2-129.
DR PDB; 2ID9; X-ray; 1.75 A; A=2-129.
DR PDB; 2IDM; X-ray; 2.00 A; A=2-129.
DR PDB; 2LP4; NMR; -; Y=2-129.
DR PDB; 3CHY; X-ray; 1.66 A; A=2-129.
DR PDB; 3F7N; X-ray; 2.00 A; A/B=2-129.
DR PDB; 3FFT; X-ray; 2.21 A; A/B=2-129.
DR PDB; 3FFW; X-ray; 2.00 A; A/B=2-129.
DR PDB; 3FFX; X-ray; 2.01 A; A/B=2-129.
DR PDB; 3FGZ; X-ray; 2.00 A; A/B=2-129.
DR PDB; 3MYY; X-ray; 2.10 A; A/B=2-129.
DR PDB; 3OLV; X-ray; 1.70 A; A/B=1-129.
DR PDB; 3OLW; X-ray; 2.30 A; A/B=1-129.
DR PDB; 3OLX; X-ray; 2.10 A; A/B=1-129.
DR PDB; 3OLY; X-ray; 2.05 A; A/B=1-129.
DR PDB; 3OO0; X-ray; 1.55 A; A/B=1-129.
DR PDB; 3OO1; X-ray; 1.70 A; A/B=1-129.
DR PDB; 3RVJ; X-ray; 2.10 A; A/B=1-129.
DR PDB; 3RVK; X-ray; 1.16 A; A=1-129.
DR PDB; 3RVL; X-ray; 1.55 A; A/B=1-129.
DR PDB; 3RVM; X-ray; 1.45 A; A=1-129.
DR PDB; 3RVN; X-ray; 2.25 A; A/B=1-129.
DR PDB; 3RVO; X-ray; 1.55 A; A=1-129.
DR PDB; 3RVP; X-ray; 2.40 A; A/B=1-129.
DR PDB; 3RVQ; X-ray; 1.15 A; A=1-129.
DR PDB; 3RVR; X-ray; 2.10 A; A/B=1-129.
DR PDB; 3RVS; X-ray; 2.10 A; A/B=1-129.
DR PDB; 5CHY; X-ray; 2.00 A; A=2-129.
DR PDB; 5D2C; X-ray; 2.06 A; A/B=2-129.
DR PDB; 5DGC; X-ray; 1.94 A; A/B=2-129.
DR PDB; 5DKF; X-ray; 1.94 A; A/B=2-129.
DR PDB; 6CHY; X-ray; 2.33 A; A/B=2-129.
DR PDB; 6TG7; X-ray; 1.65 A; A=1-129.
DR PDBsum; 1A0O; -.
DR PDBsum; 1AB5; -.
DR PDBsum; 1AB6; -.
DR PDBsum; 1BDJ; -.
DR PDBsum; 1C4W; -.
DR PDBsum; 1CEY; -.
DR PDBsum; 1CHN; -.
DR PDBsum; 1CYE; -.
DR PDBsum; 1D4Z; -.
DR PDBsum; 1DJM; -.
DR PDBsum; 1E6K; -.
DR PDBsum; 1E6L; -.
DR PDBsum; 1E6M; -.
DR PDBsum; 1EAY; -.
DR PDBsum; 1EHC; -.
DR PDBsum; 1F4V; -.
DR PDBsum; 1FFG; -.
DR PDBsum; 1FFS; -.
DR PDBsum; 1FFW; -.
DR PDBsum; 1FQW; -.
DR PDBsum; 1HEY; -.
DR PDBsum; 1JBE; -.
DR PDBsum; 1KMI; -.
DR PDBsum; 1MIH; -.
DR PDBsum; 1U8T; -.
DR PDBsum; 1UDR; -.
DR PDBsum; 1VLZ; -.
DR PDBsum; 1YMU; -.
DR PDBsum; 1YMV; -.
DR PDBsum; 1ZDM; -.
DR PDBsum; 2B1J; -.
DR PDBsum; 2ID7; -.
DR PDBsum; 2ID9; -.
DR PDBsum; 2IDM; -.
DR PDBsum; 2LP4; -.
DR PDBsum; 3CHY; -.
DR PDBsum; 3F7N; -.
DR PDBsum; 3FFT; -.
DR PDBsum; 3FFW; -.
DR PDBsum; 3FFX; -.
DR PDBsum; 3FGZ; -.
DR PDBsum; 3MYY; -.
DR PDBsum; 3OLV; -.
DR PDBsum; 3OLW; -.
DR PDBsum; 3OLX; -.
DR PDBsum; 3OLY; -.
DR PDBsum; 3OO0; -.
DR PDBsum; 3OO1; -.
DR PDBsum; 3RVJ; -.
DR PDBsum; 3RVK; -.
DR PDBsum; 3RVL; -.
DR PDBsum; 3RVM; -.
DR PDBsum; 3RVN; -.
DR PDBsum; 3RVO; -.
DR PDBsum; 3RVP; -.
DR PDBsum; 3RVQ; -.
DR PDBsum; 3RVR; -.
DR PDBsum; 3RVS; -.
DR PDBsum; 5CHY; -.
DR PDBsum; 5D2C; -.
DR PDBsum; 5DGC; -.
DR PDBsum; 5DKF; -.
DR PDBsum; 6CHY; -.
DR PDBsum; 6TG7; -.
DR AlphaFoldDB; P0AE67; -.
DR BMRB; P0AE67; -.
DR SMR; P0AE67; -.
DR BioGRID; 4259553; 314.
DR ComplexPortal; CPX-1077; Chemotaxis phosphorelay complex CheA-CheY.
DR ComplexPortal; CPX-1082; Flagellar Motor Switch Complex, CW variant.
DR ComplexPortal; CPX-1088; Chemotaxis phosphorelay complex CheY-CheZ.
DR DIP; DIP-6052N; -.
DR IntAct; P0AE67; 13.
DR STRING; 511145.b1882; -.
DR DrugBank; DB03487; (S)-Aspartimide.
DR DrugBank; DB04156; Aspartate beryllium trifluoride.
DR DrugBank; DB02461; S-Methyl Phosphocysteine.
DR iPTMnet; P0AE67; -.
DR SWISS-2DPAGE; P0AE67; -.
DR jPOST; P0AE67; -.
DR PaxDb; P0AE67; -.
DR PRIDE; P0AE67; -.
DR EnsemblBacteria; AAC74952; AAC74952; b1882.
DR EnsemblBacteria; BAA15698; BAA15698; BAA15698.
DR GeneID; 66674227; -.
DR GeneID; 946393; -.
DR KEGG; ecj:JW1871; -.
DR KEGG; eco:b1882; -.
DR PATRIC; fig|1411691.4.peg.365; -.
DR EchoBASE; EB0148; -.
DR eggNOG; COG0745; Bacteria.
DR HOGENOM; CLU_000445_69_12_6; -.
DR InParanoid; P0AE67; -.
DR OMA; AAGAHEY; -.
DR PhylomeDB; P0AE67; -.
DR BioCyc; EcoCyc:CHEY-MON; -.
DR EvolutionaryTrace; P0AE67; -.
DR PRO; PR:P0AE67; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009288; C:bacterial-type flagellum; IC:ComplexPortal.
DR GO; GO:0009433; C:bacterial-type flagellum basal body, C ring; IC:ComplexPortal.
DR GO; GO:0120107; C:bacterial-type flagellum rotor complex; IC:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0016407; F:acetyltransferase activity; IDA:CACAO.
DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IDA:EcoCyc.
DR GO; GO:0009454; P:aerotaxis; IDA:EcoCyc.
DR GO; GO:0071977; P:bacterial-type flagellum-dependent swimming motility; IDA:ComplexPortal.
DR GO; GO:0006935; P:chemotaxis; IMP:EcoCyc.
DR GO; GO:0018393; P:internal peptidyl-lysine acetylation; IDA:EcoCyc.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IDA:ComplexPortal.
DR GO; GO:0006473; P:protein acetylation; IDA:EcoliWiki.
DR GO; GO:1902021; P:regulation of bacterial-type flagellum-dependent cell motility; IDA:EcoCyc.
DR GO; GO:0050920; P:regulation of chemotaxis; IDA:ComplexPortal.
DR GO; GO:0007165; P:signal transduction; IDA:EcoCyc.
DR GO; GO:0043052; P:thermotaxis; IDA:EcoCyc.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chemotaxis; Cytoplasm;
KW Direct protein sequencing; Flagellar rotation; Magnesium; Metal-binding;
KW Phosphoprotein; Reference proteome; Two-component regulatory system.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..129
FT /note="Chemotaxis protein CheY"
FT /id="PRO_0000081040"
FT DOMAIN 7..124
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT BINDING 12
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:8176739"
FT BINDING 13
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 57
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:8176739"
FT BINDING 59
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:8176739"
FT MOD_RES 57
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169,
FT ECO:0000269|PubMed:1869568, ECO:0000269|PubMed:2689446"
FT MOD_RES 92
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:11359578,
FT ECO:0000269|PubMed:9560203"
FT MOD_RES 109
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:1390767,
FT ECO:0000269|PubMed:9560203"
FT MUTAGEN 12
FT /note="D->A: Abolishes magnesium binding."
FT /evidence="ECO:0000269|PubMed:11023787"
FT MUTAGEN 13
FT /note="D->A: No effect on magnesium binding."
FT /evidence="ECO:0000269|PubMed:11023787"
FT MUTAGEN 57
FT /note="D->A: Abolishes magnesium binding."
FT /evidence="ECO:0000269|PubMed:11023787"
FT MUTAGEN 87
FT /note="T->I: Impairs chemotaxis; when associated with W-
FT 106."
FT MUTAGEN 92
FT /note="K->R: No effect on chemotaxis."
FT /evidence="ECO:0000269|PubMed:9560203"
FT MUTAGEN 95
FT /note="I->A,V: Enhanced CW flagellar rotational signaling
FT activity."
FT MUTAGEN 95
FT /note="I->D,K,M: Loss of CW flagellar rotational signaling
FT activity."
FT MUTAGEN 106
FT /note="Y->W: Impairs chemotaxis; when associated with I-
FT 87."
FT CONFLICT 113
FT /note="A -> P (in Ref. 2; AAA23570)"
FT /evidence="ECO:0000305"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:3RVL"
FT STRAND 8..11
FT /evidence="ECO:0007829|PDB:1JBE"
FT HELIX 15..27
FT /evidence="ECO:0007829|PDB:1JBE"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:1JBE"
FT HELIX 39..46
FT /evidence="ECO:0007829|PDB:1JBE"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:1CEY"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:1JBE"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:1JBE"
FT HELIX 65..73
FT /evidence="ECO:0007829|PDB:1JBE"
FT TURN 76..80
FT /evidence="ECO:0007829|PDB:3RVQ"
FT STRAND 83..89
FT /evidence="ECO:0007829|PDB:1JBE"
FT HELIX 92..100
FT /evidence="ECO:0007829|PDB:1JBE"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:1JBE"
FT HELIX 113..127
FT /evidence="ECO:0007829|PDB:1JBE"
SQ SEQUENCE 129 AA; 14097 MW; E4B60B8A73DA14DC CRC64;
MADKELKFLV VDDFSTMRRI VRNLLKELGF NNVEEAEDGV DALNKLQAGG YGFVISDWNM
PNMDGLELLK TIRADGAMSA LPVLMVTAEA KKENIIAAAQ AGASGYVVKP FTAATLEEKL
NKIFEKLGM
