SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P0AE67

- CHEY_ECOLI

UniProt

P0AE67 - CHEY_ECOLI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Chemotaxis protein CheY
Gene
cheY, b1882, JW1871
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. In its active (phosphorylated or acetylated) form, CheY exhibits enhanced binding to a switch component, FliM, at the flagellar motor which induces a change from counterclockwise to clockwise flagellar rotation. Overexpression of CheY in association with MotA and MotB improves motility of a ycgR disruption, suggesting there is an interaction (direct or indirect) between the c-di-GMP-binding flagellar brake protein and the flagellar stator.1 Publication

Cofactori

Binds 1 magnesium ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi12 – 121Magnesium1 Publication
Metal bindingi13 – 131Magnesium
Metal bindingi57 – 571Magnesium1 Publication
Metal bindingi59 – 591Magnesium; via carbonyl oxygen1 Publication

GO - Molecular functioni

  1. acetyltransferase activity Source: CACAO
  2. magnesium ion binding Source: EcoCyc
  3. phosphorelay response regulator activity Source: InterPro
  4. protein binding Source: IntAct

GO - Biological processi

  1. bacterial-type flagellum-dependent cell motility Source: EcoCyc
  2. chemotaxis Source: EcoCyc
  3. internal peptidyl-lysine acetylation Source: CACAO
  4. phosphorelay signal transduction system Source: EcoCyc
  5. protein acetylation Source: EcoCyc
Complete GO annotation...

Keywords - Biological processi

Chemotaxis, Flagellar rotation, Two-component regulatory system

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:CHEY-MONOMER.
ECOL316407:JW1871-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Chemotaxis protein CheY
Gene namesi
Name:cheY
Ordered Locus Names:b1882, JW1871
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10150. cheY.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi12 – 121D → A: Abolishes magnesium binding. 1 Publication
Mutagenesisi13 – 131D → A: No effect on magnesium binding. 1 Publication
Mutagenesisi57 – 571D → A: Abolishes magnesium binding. 1 Publication
Mutagenesisi87 – 871T → I: Impairs chemotaxis; when associated with W-106.
Mutagenesisi92 – 921K → R: No effect on chemotaxis. 1 Publication
Mutagenesisi95 – 951I → A or V: Enhanced CW flagellar rotational signaling activity.
Mutagenesisi95 – 951I → D, K or M: Loss of CW flagellar rotational signaling activity.
Mutagenesisi106 – 1061Y → W: Impairs chemotaxis; when associated with I-87.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 129128Chemotaxis protein CheY
PRO_0000081040Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei57 – 5714-aspartylphosphate1 Publication
Modified residuei92 – 921N6-acetyllysine2 Publications
Modified residuei109 – 1091N6-acetyllysine2 Publications

Post-translational modificationi

Phosphorylated by CheA or acetylated by acetyl-CoA synthetase, depending on which acetate metabolism pathway is available. The major acetylation site seems to be Lys-92. Dephosphorylated (inactivated) by CheZ.4 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP0AE67.
PRIDEiP0AE67.

2D gel databases

SWISS-2DPAGEP0AE67.

Expressioni

Gene expression databases

GenevestigatoriP0AE67.

Interactioni

Subunit structurei

Interacts (phosphorylated CheY) with CheZ (via C-terminus).

Binary interactionsi

WithEntry#Exp.IntActNotes
cheAP073633EBI-546693,EBI-1026773
cheZP0A9H93EBI-546693,EBI-546726

Protein-protein interaction databases

DIPiDIP-48237N.
IntActiP0AE67. 12 interactions.
STRINGi511145.b1882.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 53
Beta strandi8 – 114
Helixi15 – 2713
Beta strandi33 – 386
Helixi39 – 468
Turni47 – 493
Beta strandi53 – 586
Beta strandi61 – 633
Helixi65 – 739
Turni76 – 805
Beta strandi83 – 897
Helixi92 – 1009
Beta strandi104 – 1107
Helixi113 – 12715

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A0OX-ray2.95A/C/E/G2-129[»]
1AB5X-ray2.40A/B5-129[»]
1AB6X-ray2.20A/B5-129[»]
1BDJX-ray2.68A2-129[»]
1C4WX-ray1.84A2-129[»]
1CEYNMR-A2-129[»]
1CHNX-ray1.76A2-129[»]
1CYENMR-A3-129[»]
1D4ZX-ray1.90A2-129[»]
1DJMNMR-A1-129[»]
1E6KX-ray2.00A3-129[»]
1E6LX-ray1.90A3-129[»]
1E6MX-ray1.70A3-129[»]
1EAYX-ray2.00A/B2-129[»]
1EHCX-ray2.26A2-129[»]
1F4VX-ray2.22A/B/C2-129[»]
1FFGX-ray2.10A/C2-129[»]
1FFSX-ray2.40A/C2-129[»]
1FFWX-ray2.70A/C2-129[»]
1FQWX-ray2.37A/B2-129[»]
1HEYX-ray2.24A2-129[»]
1JBEX-ray1.08A2-129[»]
1KMIX-ray2.90Y1-129[»]
1MIHX-ray2.70A/B1-129[»]
1U8TX-ray1.50A/B/C/D2-129[»]
1UDRX-ray1.90A/B/C/D1-129[»]
1VLZX-ray2.05A/B2-129[»]
1YMUX-ray2.30A/B3-129[»]
1YMVX-ray1.90A3-129[»]
1ZDMX-ray2.40A/B1-129[»]
2B1JX-ray2.40A/B2-129[»]
2ID7X-ray1.75A2-129[»]
2ID9X-ray1.75A2-129[»]
2IDMX-ray2.00A2-129[»]
2LP4NMR-Y2-129[»]
3CHYX-ray1.66A2-129[»]
3F7NX-ray2.00A/B2-129[»]
3FFTX-ray2.21A/B2-129[»]
3FFWX-ray2.00A/B2-129[»]
3FFXX-ray2.01A/B2-129[»]
3FGZX-ray2.00A/B2-129[»]
3MYYX-ray2.10A/B2-129[»]
3OLVX-ray1.70A/B1-129[»]
3OLWX-ray2.30A/B1-129[»]
3OLXX-ray2.10A/B1-129[»]
3OLYX-ray2.05A/B1-129[»]
3OO0X-ray1.55A/B1-129[»]
3OO1X-ray1.70A/B1-129[»]
3RVJX-ray2.10A/B1-129[»]
3RVKX-ray1.16A1-129[»]
3RVLX-ray1.55A/B1-129[»]
3RVMX-ray1.45A1-129[»]
3RVNX-ray2.25A/B1-129[»]
3RVOX-ray1.55A1-129[»]
3RVPX-ray2.40A/B1-129[»]
3RVQX-ray1.15A1-129[»]
3RVRX-ray2.10A/B1-129[»]
3RVSX-ray2.10A/B1-129[»]
5CHYX-ray2.00A2-129[»]
6CHYX-ray2.33A/B2-129[»]
ProteinModelPortaliP0AE67.
SMRiP0AE67. Positions 2-129.

Miscellaneous databases

EvolutionaryTraceiP0AE67.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 124118Response regulatory
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0784.
HOGENOMiHOG000034820.
KOiK03413.
OMAiGSCARIR.
OrthoDBiEOG6PKFC7.
PhylomeDBiP0AE67.

Family and domain databases

InterProiIPR011006. CheY-like_superfamily.
IPR001789. Sig_transdc_resp-reg_receiver.
[Graphical view]
PfamiPF00072. Response_reg. 1 hit.
[Graphical view]
SMARTiSM00448. REC. 1 hit.
[Graphical view]
SUPFAMiSSF52172. SSF52172. 1 hit.
PROSITEiPS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0AE67-1 [UniParc]FASTAAdd to Basket

« Hide

MADKELKFLV VDDFSTMRRI VRNLLKELGF NNVEEAEDGV DALNKLQAGG    50
YGFVISDWNM PNMDGLELLK TIRADGAMSA LPVLMVTAEA KKENIIAAAQ 100
AGASGYVVKP FTAATLEEKL NKIFEKLGM 129
Length:129
Mass (Da):14,097
Last modified:January 23, 2007 - v2
Checksum:iE4B60B8A73DA14DC
GO

Mass spectrometryi

Molecular mass is 13966 Da from positions 2 - 129. Determined by ESI. 1 Publication
Molecular mass is 14008 Da from positions 2 - 129. Determined by ESI. With N6-acetyl-Lys-92.1 Publication

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti113 – 1131A → P in AAA23570. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
K02175 Genomic DNA. Translation: AAA23577.1.
M13463 Genomic DNA. Translation: AAA23570.1.
U00096 Genomic DNA. Translation: AAC74952.1.
AP009048 Genomic DNA. Translation: BAA15698.1.
PIRiE25195. QRECCY.
RefSeqiNP_416396.1. NC_000913.3.
YP_490144.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74952; AAC74952; b1882.
BAA15698; BAA15698; BAA15698.
GeneIDi12930559.
946393.
KEGGiecj:Y75_p1858.
eco:b1882.
PATRICi32119091. VBIEscCol129921_1963.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
K02175 Genomic DNA. Translation: AAA23577.1 .
M13463 Genomic DNA. Translation: AAA23570.1 .
U00096 Genomic DNA. Translation: AAC74952.1 .
AP009048 Genomic DNA. Translation: BAA15698.1 .
PIRi E25195. QRECCY.
RefSeqi NP_416396.1. NC_000913.3.
YP_490144.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A0O X-ray 2.95 A/C/E/G 2-129 [» ]
1AB5 X-ray 2.40 A/B 5-129 [» ]
1AB6 X-ray 2.20 A/B 5-129 [» ]
1BDJ X-ray 2.68 A 2-129 [» ]
1C4W X-ray 1.84 A 2-129 [» ]
1CEY NMR - A 2-129 [» ]
1CHN X-ray 1.76 A 2-129 [» ]
1CYE NMR - A 3-129 [» ]
1D4Z X-ray 1.90 A 2-129 [» ]
1DJM NMR - A 1-129 [» ]
1E6K X-ray 2.00 A 3-129 [» ]
1E6L X-ray 1.90 A 3-129 [» ]
1E6M X-ray 1.70 A 3-129 [» ]
1EAY X-ray 2.00 A/B 2-129 [» ]
1EHC X-ray 2.26 A 2-129 [» ]
1F4V X-ray 2.22 A/B/C 2-129 [» ]
1FFG X-ray 2.10 A/C 2-129 [» ]
1FFS X-ray 2.40 A/C 2-129 [» ]
1FFW X-ray 2.70 A/C 2-129 [» ]
1FQW X-ray 2.37 A/B 2-129 [» ]
1HEY X-ray 2.24 A 2-129 [» ]
1JBE X-ray 1.08 A 2-129 [» ]
1KMI X-ray 2.90 Y 1-129 [» ]
1MIH X-ray 2.70 A/B 1-129 [» ]
1U8T X-ray 1.50 A/B/C/D 2-129 [» ]
1UDR X-ray 1.90 A/B/C/D 1-129 [» ]
1VLZ X-ray 2.05 A/B 2-129 [» ]
1YMU X-ray 2.30 A/B 3-129 [» ]
1YMV X-ray 1.90 A 3-129 [» ]
1ZDM X-ray 2.40 A/B 1-129 [» ]
2B1J X-ray 2.40 A/B 2-129 [» ]
2ID7 X-ray 1.75 A 2-129 [» ]
2ID9 X-ray 1.75 A 2-129 [» ]
2IDM X-ray 2.00 A 2-129 [» ]
2LP4 NMR - Y 2-129 [» ]
3CHY X-ray 1.66 A 2-129 [» ]
3F7N X-ray 2.00 A/B 2-129 [» ]
3FFT X-ray 2.21 A/B 2-129 [» ]
3FFW X-ray 2.00 A/B 2-129 [» ]
3FFX X-ray 2.01 A/B 2-129 [» ]
3FGZ X-ray 2.00 A/B 2-129 [» ]
3MYY X-ray 2.10 A/B 2-129 [» ]
3OLV X-ray 1.70 A/B 1-129 [» ]
3OLW X-ray 2.30 A/B 1-129 [» ]
3OLX X-ray 2.10 A/B 1-129 [» ]
3OLY X-ray 2.05 A/B 1-129 [» ]
3OO0 X-ray 1.55 A/B 1-129 [» ]
3OO1 X-ray 1.70 A/B 1-129 [» ]
3RVJ X-ray 2.10 A/B 1-129 [» ]
3RVK X-ray 1.16 A 1-129 [» ]
3RVL X-ray 1.55 A/B 1-129 [» ]
3RVM X-ray 1.45 A 1-129 [» ]
3RVN X-ray 2.25 A/B 1-129 [» ]
3RVO X-ray 1.55 A 1-129 [» ]
3RVP X-ray 2.40 A/B 1-129 [» ]
3RVQ X-ray 1.15 A 1-129 [» ]
3RVR X-ray 2.10 A/B 1-129 [» ]
3RVS X-ray 2.10 A/B 1-129 [» ]
5CHY X-ray 2.00 A 2-129 [» ]
6CHY X-ray 2.33 A/B 2-129 [» ]
ProteinModelPortali P0AE67.
SMRi P0AE67. Positions 2-129.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-48237N.
IntActi P0AE67. 12 interactions.
STRINGi 511145.b1882.

2D gel databases

SWISS-2DPAGE P0AE67.

Proteomic databases

PaxDbi P0AE67.
PRIDEi P0AE67.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74952 ; AAC74952 ; b1882 .
BAA15698 ; BAA15698 ; BAA15698 .
GeneIDi 12930559.
946393.
KEGGi ecj:Y75_p1858.
eco:b1882.
PATRICi 32119091. VBIEscCol129921_1963.

Organism-specific databases

EchoBASEi EB0148.
EcoGenei EG10150. cheY.

Phylogenomic databases

eggNOGi COG0784.
HOGENOMi HOG000034820.
KOi K03413.
OMAi GSCARIR.
OrthoDBi EOG6PKFC7.
PhylomeDBi P0AE67.

Enzyme and pathway databases

BioCyci EcoCyc:CHEY-MONOMER.
ECOL316407:JW1871-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0AE67.
PROi P0AE67.

Gene expression databases

Genevestigatori P0AE67.

Family and domain databases

InterProi IPR011006. CheY-like_superfamily.
IPR001789. Sig_transdc_resp-reg_receiver.
[Graphical view ]
Pfami PF00072. Response_reg. 1 hit.
[Graphical view ]
SMARTi SM00448. REC. 1 hit.
[Graphical view ]
SUPFAMi SSF52172. SSF52172. 1 hit.
PROSITEi PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Overexpression and sequence of the Escherichia coli cheY gene and biochemical activities of the CheY protein."
    Matsumura P., Rydel J.J., Linzmeier R., Vacante D.
    J. Bacteriol. 160:36-41(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Nucleotide sequence corresponding to five chemotaxis genes in Escherichia coli."
    Mutoh N., Simon M.I.
    J. Bacteriol. 165:161-166(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Phosphorylation of three proteins in the signaling pathway of bacterial chemotaxis."
    Hess J.F., Oosawa K., Kaplan N., Simon M.I.
    Cell 53:79-87(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION.
  7. "Identification of the site of phosphorylation of the chemotaxis response regulator protein, CheY."
    Sanders D.A., Gillece-Castro B.L., Stock A.M., Burlingame A.L., Koshland D.E. Jr.
    J. Biol. Chem. 264:21770-21778(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT ASP-57, PARTIAL PROTEIN SEQUENCE.
  8. "Acetyladenylate or its derivative acetylates the chemotaxis protein CheY in vitro and increases its activity at the flagellar switch."
    Barak R., Welch M., Yanovsky A., Oosawa K., Eisenbach M.
    Biochemistry 31:10099-10107(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-109.
  9. "Characterization of the CheAS/CheZ complex: a specific interaction resulting in enhanced dephosphorylating activity on CheY-phosphate."
    Wang H., Matsumura P.
    Mol. Microbiol. 19:695-703(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEPHOSPHORYLATION BY CHEAS/CHEZ COMPLEX.
  10. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  11. "Acetylation at Lys-92 enhances signaling by the chemotaxis response regulator protein CheY."
    Ramakrishnan R., Schuster M., Bourret R.B.
    Proc. Natl. Acad. Sci. U.S.A. 95:4918-4923(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-92 AND LYS-109 BY ACETYL-COA SYNTHETASE, MASS SPECTROMETRY, MUTAGENESIS OF LYS-92.
  12. "Acetylation of the response regulator, CheY, is involved in bacterial chemotaxis."
    Barak R., Eisenbach M.
    Mol. Microbiol. 40:731-743(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT OF ACETYLATION AT LYS-92 IN CHEMOTAXIS.
  13. "Kinetic characterization of catalysis by the chemotaxis phosphatase CheZ. Modulation of activity by the phosphorylated CheY substrate."
    Silversmith R.E., Levin M.D., Schilling E., Bourret R.B.
    J. Biol. Chem. 283:756-765(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEPHOSPHORYLATION BY CHEZ.
  14. "The c-di-GMP binding protein YcgR controls flagellar motor direction and speed to affect chemotaxis by a 'backstop brake' mechanism."
    Paul K., Nieto V., Carlquist W.C., Blair D.F., Harshey R.M.
    Mol. Cell 38:128-139(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: K12 / RP3098.
  15. "Crystal structure of Escherichia coli CheY refined at 1.7-A resolution."
    Volz K., Matsumura P.
    J. Biol. Chem. 266:15511-15519(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
  16. "Magnesium binding to the bacterial chemotaxis protein CheY results in large conformational changes involving its functional surface."
    Bellsolell L., Prieto J., Serrano L., Coll M.
    J. Mol. Biol. 238:489-495(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS).
  17. Erratum
    Bellsolell L., Prieto J., Serrano L., Coll M.
    J. Mol. Biol. 242:103-103(1994)
  18. "The three-dimensional structure of two mutants of the signal transduction protein CheY suggest its molecular activation mechanism."
    Bellsolell L., Cronet P., Majolero M., Serrano L., Coll M.
    J. Mol. Biol. 257:116-128(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANTS GLY-17 AND GLY-14/GLY-15/GLY-17.
  19. "Crystal structures of CheY mutants Y106W and T87I/Y106W. CheY activation correlates with movement of residue 106."
    Zhu X., Rebello J., Matsumura P., Volz K.
    J. Biol. Chem. 272:5000-5006(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANTS TRP-106 AND ILE-87/TRP-106.
  20. "Structure analysis of two CheY mutants: importance of the hydrogen-bond contribution to protein stability."
    Wilcock D., Pisabarro M.T., Lopez-Hernandez E., Serrano L., Coll M.
    Acta Crystallogr. D 54:378-385(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
  21. "Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY."
    Welch M., Chinardet N., Mourey L., Birck C., Samama J.-P.
    Nat. Struct. Biol. 5:25-29(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH CHEA.
  22. "Two binding modes reveal flexibility in kinase/response regulator interactions in the bacterial chemotaxis pathway."
    McEvoy M.M., Hausrath A.C., Randolph G.B., Remington S.J., Dahlquist F.W.
    Proc. Natl. Acad. Sci. U.S.A. 95:7333-7338(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
  23. "Correlated switch binding and signaling in bacterial chemotaxis."
    Schuster M., Zhao R., Bourret R.B., Collins E.J.
    J. Biol. Chem. 275:19752-19758(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANT VAL-95.
  24. "Crystallization of a complex between a novel C-terminal transmitter, HPt domain, of the anaerobic sensor kinase ArcB and the chemotaxis response regulator CheY."
    Kato M., Mizuno T., Hakoshima T.
    Acta Crystallogr. D 54:140-142(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF COMPLEX WITH ARCB.
  25. "Towards understanding a molecular switch mechanism: thermodynamic and crystallographic studies of the signal transduction protein CheY."
    Sola M., Lopez-Hernandez E., Cronet P., Lacroix E., Serrano L., Coll M., Parraga A.
    J. Mol. Biol. 303:213-225(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), MUTAGENESIS OF ASP-12; ASP-13 AND ASP-57.
  26. "Structure and catalytic mechanism of the E. coli chemotaxis phosphatase CheZ."
    Zhao R., Collins E.J., Bourret R.B., Silversmith R.E.
    Nat. Struct. Biol. 9:570-575(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH CHEZ.
  27. "1H- and 15N-NMR assignment and solution structure of the chemotactic Escherichia coli Che Y protein."
    Bruix M., Pascual J., Santoro J., Prieto J., Serrano L., Rico M.
    Eur. J. Biochem. 215:573-585(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  28. Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiCHEY_ECOLI
AccessioniPrimary (citable) accession number: P0AE67
Secondary accession number(s): P06143
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi