P0A2D5 (CHEY_SALTY) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Chemotaxis protein CheY

Gene names

Name:	cheY
Ordered Locus Names:	STM1916

Organism

Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]

Taxonomic identifier

99287 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella › Salmonella choleraesuis › Salmonella enterica I › Salmonella typhimurium

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. Shows autophosphatase activity which is enhanced by CheZ.
Cofactor	Binds 1 magnesium ion per subunit.
Subunit structure	Interacts (phosphorylated CheY) with CheZ (via C-terminus). Ref.6
Subcellular location	Cytoplasm.
Post-translational modification	Phosphorylated by CheA or acetylated by acetyl-CoA synthetase, depending on which acetate metabolism pathway is available By similarity. Dephosphorylated (inactivated) by CheZ. Ref.3 Ref.4 Ref.5 Ref.7
Sequence similarities	Contains 1 response regulatory domain.

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 Reference proteome
Gene Ontology (GO)
Biological_process	chemotaxis Inferred from electronic annotation. Source: UniProtKB-KW ciliary or flagellar motility Inferred from electronic annotation. Source: UniProtKB-KW intracellular signal transduction Inferred from electronic annotation. Source: GOC regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphorelay response regulator activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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_0000081045

Regions

Domain

7 – 124

118

Response regulatory

Sites

Metal binding

12

1

Magnesium

Metal binding

13

1

Magnesium

Metal binding

57

1

Magnesium

Metal binding

59

1

Magnesium; via carbonyl oxygen

Amino acid modifications

Modified residue

57

1

4-aspartylphosphate

Modified residue

92

1

N6-acetyllysine By similarity

Modified residue

109

1

N6-acetyllysine By similarity

Experimental info

Mutagenesis

13

1

D → N: Abolishes function, reduced rate of phosphorylation and affinity for magnesium ion. Ref.4

Mutagenesis

14

1

F → A: Diminished rate of phosphorylation. Ref.10

Mutagenesis

57

1

D → N: Abolishes function and phosphorylation. Ref.4

Mutagenesis

59

1

N → A: Diminished rate of phosphorylation. Ref.10

Mutagenesis

109

1

K → R: Abolishes function, decreased autophosphatase activity. Ref.4

Secondary structure

1

.

.

.

.

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.

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.

.

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129

Helix Strand Turn

Details...

Beta strand

8 – 11

4

Helix

15 – 28

14

Beta strand

33 – 38

6

Helix

39 – 46

8

Beta strand

53 – 58

6

Beta strand

61 – 63

3

Helix

65 – 74

10

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)
	P0A2D5 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: A0B4712E18626207	FASTA	129	14,125
	10 20 30 40 50 60 MADKELKFLV VDDFSTMRRI VRNLLKELGF NNVEEAEDGV DALNKLQAGG FGFIISDWNM 70 80 90 100 110 120 PNMDGLELLK TIRADSAMSA LPVLMVTAEA KKENIIAAAQ AGASGYVVKP FTAATLEEKL NKIFEKLGM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Homologies between the Salmonella typhimurium CheY protein and proteins involved in the regulation of chemotaxis, membrane protein synthesis, and sporulation." Stock A., Koshland D.E. Jr., Stock J. Proc. Natl. Acad. Sci. U.S.A. 82:7989-7993(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2." McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K. Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LT2 / SGSC1412 / ATCC 700720.
[3]	"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 AT ASP-57.
[4]	"Roles of the highly conserved aspartate and lysine residues in the response regulator of bacterial chemotaxis." Lukat G.S., Lee B.H., Mottonen J.M., Stock A.M., Stock J.B. J. Biol. Chem. 266:8348-8354(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT ASP-57, MUTAGENESIS OF ASP-13; ASP-57 AND LYS-109.
[5]	"Signal termination in bacterial chemotaxis: CheZ mediates dephosphorylation of free rather than switch-bound CheY." Bren A., Welch M., Blat Y., Eisenbach M. Proc. Natl. Acad. Sci. U.S.A. 93:10090-10093(1996) [PubMed] [Europe PMC] [Abstract] Cited for: DEPHOSPHORYLATION BY CHEZ.
[6]	"Regulation of phosphatase activity in bacterial chemotaxis." Blat Y., Gillespie B., Bren A., Dahlquist F.W., Eisenbach M. J. Mol. Biol. 284:1191-1199(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CHEZ.
[7]	"Mechanism of phosphatase activity in the chemotaxis response regulator CheY." Wolanin P.M., Webre D.J., Stock J.B. Biochemistry 42:14075-14082(2003) [PubMed] [Europe PMC] [Abstract] Cited for: DEPHOSPHORYLATION BY CHEZ.
[8]	"Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis." Stock A.M., Mottonen J.M., Stock J.B., Schutt C.E. Nature 337:745-749(1989) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
[9]	"Structure of the Mg(2+)-bound form of CheY and mechanism of phosphoryl transfer in bacterial chemotaxis." Stock A.M., Martinez-Hackert E., Rasmussen B.F., West A.H., Stock J.B., Ringe D., Petsko G.A. Biochemistry 32:13375-13380(1993) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[10]	"Crystal structures of beryllium fluoride-free and beryllium fluoride-bound CheY in complex with the conserved C-terminal peptide of CheZ reveal dual binding modes specific to CheY conformation." Guhaniyogi J., Robinson V.L., Stock A.M. J. Mol. Biol. 359:624-645(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH CHEZ, MUTAGENESIS OF PHE-14 AND ASN-59.
[11]	"Interaction of CheY with the C-terminal peptide of CheZ." Guhaniyogi J., Wu T., Patel S.S., Stock A.M. J. Bacteriol. 190:1419-1428(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.69 ANGSTROMS) IN COMPLEX WITH CHEZ.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M12131 Genomic DNA. Translation: AAA27037.1.
AE006468 Genomic DNA. Translation: AAL20832.1.

PIR

QREBCY. A23567.

RefSeq

NP_460873.1. NC_003197.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CHE	X-ray	1.80	A	2-129	[»]
2CHF	X-ray	1.80	A	2-129	[»]
2CHY	X-ray	2.70	A	2-129	[»]
2FKA	X-ray	2.00	A	2-128	[»]
2FLK	X-ray	2.10	A	2-128	[»]
2FLW	X-ray	2.00	A	2-128	[»]
2FMF	X-ray	2.00	A	2-128	[»]
2FMH	X-ray	2.00	A	2-128	[»]
2FMI	X-ray	2.30	A	2-128	[»]
2FMK	X-ray	2.00	A	2-128	[»]
2PL9	X-ray	2.60	A/B/C	2-129	[»]
2PMC	X-ray	2.69	A/B/C/D	2-129	[»]

ProteinModelPortal

P0A2D5.

SMR

P0A2D5. Positions 2-129.

ModBase

Search...

Protein-protein interaction databases

STRING

99287.STM1916.

Proteomic databases

PaxDb

P0A2D5.

PRIDE

P0A2D5.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAL20832; AAL20832; STM1916.

GeneID

1253437.

KEGG

stm:STM1916.

PATRIC

32382387. VBISalEnt20916_2032.

Phylogenomic databases

eggNOG

COG0784.

HOGENOM

HOG000034820.

KO

K03413.

OMA

GHDEELH.

ProtClustDB

PRK10610.

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

P0A2D5.

Entry information

Entry name

CHEY_SALTY

Accession

Primary (citable) accession number: P0A2D5
Secondary accession number(s): P06657

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 69 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program