P0AE67 (CHEY_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Chemotaxis protein CheY

Gene names

Name:	cheY
Ordered Locus Names:	b1882, JW1871

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	129 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.14
Cofactor	Binds 1 magnesium ion per subunit.
Subunit structure	Interacts (phosphorylated CheY) with CheZ (via C-terminus).
Subcellular location	Cytoplasm.
Post-translational modification	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. Ref.6 Ref.7 Ref.9 Ref.13
Sequence similarities	Contains 1 response regulatory domain.
Mass spectrometry	Molecular mass is 13966 Da from positions 2 - 129. Determined by ESI. Ref.11 Molecular mass is 14008 Da from positions 2 - 129. Determined by ESI. With N6-acetyl-Lys-92. Ref.11

Ontologies

Keywords
Biological process	Chemotaxis Flagellar rotation Two-component regulatory system
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	chemotaxis Inferred from mutant phenotype Ref.12. Source: EcoCyc flagellar cell motility Traceable author statement PubMed 8809743. Source: EcoCyc intracellular signal transduction Inferred from electronic annotation. Source: GOC phosphorelay signal transduction system Inferred from direct assay Ref.6. Source: EcoCyc protein acetylation Inferred from direct assay PubMed 16630631. Source: EcoCyc regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	magnesium ion binding Inferred from mutant phenotype PubMed 2201404. Source: EcoCyc phosphorelay response regulator activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
cheA	P07363	3	EBI-546693,EBI-1026773
cheZ	P0A9H9	3	EBI-546693,EBI-546726

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 129

128

Chemotaxis protein CheY

PRO_0000081040

Regions

Domain

7 – 124

118

Response regulatory

Sites

Metal binding

12

1

Magnesium Ref.16

Metal binding

13

1

Magnesium

Metal binding

57

1

Magnesium Ref.16

Metal binding

59

1

Magnesium; via carbonyl oxygen Ref.16

Amino acid modifications

Modified residue

57

1

4-aspartylphosphate Ref.15

Modified residue

92

1

N6-acetyllysine Ref.11 Ref.12

Modified residue

109

1

N6-acetyllysine Ref.8 Ref.11

Experimental info

Mutagenesis

12

1

D → A: Abolishes magnesium binding. Ref.25

Mutagenesis

13

1

D → A: No effect on magnesium binding. Ref.25

Mutagenesis

57

1

D → A: Abolishes magnesium binding. Ref.25

Mutagenesis

87

1

T → I: Impairs chemotaxis; when associated with W-106.

Mutagenesis

92

1

K → R: No effect on chemotaxis. Ref.11

Mutagenesis

95

1

I → A or V: Enhanced CW flagellar rotational signaling activity.

Mutagenesis

95

1

I → D, K or M: Loss of CW flagellar rotational signaling activity.

Mutagenesis

106

1

Y → W: Impairs chemotaxis; when associated with I-87.

Sequence conflict

113

1

A → P in AAA23570. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

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.

.

.

.

.

.

.

.

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.

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.

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129

Helix Strand Turn

Details...

Helix

3 – 5

3

Beta strand

8 – 11

4

Helix

15 – 27

13

Beta strand

33 – 38

6

Helix

39 – 46

8

Turn

47 – 49

3

Beta strand

53 – 58

6

Beta strand

61 – 63

3

Helix

65 – 73

9

Turn

76 – 80

5

Beta strand

83 – 89

7

Helix

92 – 100

9

Beta strand

104 – 110

7

Helix

113 – 127

15

Sequences

	Sequence		Length	Mass (Da)
	P0AE67 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: E4B60B8A73DA14DC	FASTA	129	14,097
	10 20 30 40 50 60 MADKELKFLV VDDFSTMRRI VRNLLKELGF NNVEEAEDGV DALNKLQAGG YGFVISDWNM 70 80 90 100 110 120 PNMDGLELLK TIRADGAMSA LPVLMVTAEA KKENIIAAAQ AGASGYVVKP FTAATLEEKL NKIFEKLGM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map." Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S. , Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., Horiuchi T. DNA Res. 3:379-392(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] 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]	"NMR structure of activated CheY." Cho H.S., Lee S.-Y., Yan D., Pan X., Parkinson J.S., Kustu S., Wemmer D.E., Pelton J.G. J. Mol. Biol. 297:543-551(2000) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

K02175 Genomic DNA. Translation: AAA23577.1.
M13463 Genomic DNA. Translation: AAA23570.1.
U00096 Genomic DNA. Translation: AAC74952.1.
AP009048 Genomic DNA. Translation: BAA15698.1.

PIR

QRECCY. E25195.

RefSeq

NP_416396.1. NC_000913.2.
YP_490144.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	3-129	[»]
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	2-128	[»]
2ID7	X-ray	1.75	A	2-128	[»]
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	[»]

ProteinModelPortal

P0AE67.

SMR

P0AE67. Positions 2-129.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48237N.

IntAct

P0AE67. 12 interactions.

STRING

511145.b1882.

2D gel databases

SWISS-2DPAGE

P0AE67.

Proteomic databases

PaxDb

P0AE67.

PRIDE

P0AE67.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC74952; AAC74952; b1882.
BAA15698; BAA15698; BAA15698.

GeneID

12930559.
946393.

KEGG

ecj:Y75_p1858.
eco:b1882.

PATRIC

32119091. VBIEscCol129921_1963.

Organism-specific databases

EchoBASE

EB0148.

EcoGene

EG10150. cheY.

Phylogenomic databases

eggNOG

COG0784.

HOGENOM

HOG000034820.

KO

K03413.

OMA

FGFVISD.

ProtClustDB

PRK10610.

Enzyme and pathway databases

BioCyc

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

Gene expression databases

Genevestigator

P0AE67.

Family and domain databases

InterPro

IPR011006. CheY-like_superfamily.
IPR001789. Sig_transdc_resp-reg_receiver.
[Graphical view]

Pfam

PF00072. Response_reg. 1 hit.
[Graphical view]

SMART

SM00448. REC. 1 hit.
[Graphical view]

SUPFAM

SSF52172. CheY_like. 1 hit.

PROSITE

PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0AE67.

Entry information

Entry name

CHEY_ECOLI

Accession

Primary (citable) accession number: P0AE67
Secondary accession number(s): P06143

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 83 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program