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Protein

Chemotaxis protein CheY

Gene

cheY

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: 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. Shows autophosphatase activity which is enhanced by CheZ.

Cofactori

Mg2+Note: Binds 1 Mg2+ ion per subunit.

Sites

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

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. archaeal or bacterial-type flagellum-dependent cell motility Source: UniProtKB-KW
  2. chemotaxis Source: UniProtKB-KW
  3. phosphorelay signal transduction system Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Chemotaxis, Flagellar rotation, Two-component regulatory system

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciSENT99287:GCTI-1928-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Chemotaxis protein CheY
Gene namesi
Name:cheY
Ordered Locus Names:STM1916
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
ProteomesiUP000001014 Componenti: Chromosome

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
Mutagenesisi13 – 131D → N: Abolishes function, reduced rate of phosphorylation and affinity for magnesium ion. 1 Publication
Mutagenesisi14 – 141F → A: Diminished rate of phosphorylation. 1 Publication
Mutagenesisi57 – 571D → N: Abolishes function and phosphorylation. 1 Publication
Mutagenesisi59 – 591N → A: Diminished rate of phosphorylation. 1 Publication
Mutagenesisi109 – 1091K → R: Abolishes function, decreased autophosphatase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 129128Chemotaxis protein CheYPRO_0000081045Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei57 – 5714-aspartylphosphatePROSITE-ProRule annotation2 Publications
Modified residuei92 – 921N6-acetyllysineBy similarity
Modified residuei109 – 1091N6-acetyllysineBy similarity

Post-translational modificationi

Phosphorylated by CheA or acetylated by acetyl-CoA synthetase, depending on which acetate metabolism pathway is available (By similarity). Dephosphorylated (inactivated) by CheZ.By similarity2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP0A2D5.
PRIDEiP0A2D5.

Interactioni

Subunit structurei

Interacts (phosphorylated CheY) with CheZ (via C-terminus).3 Publications

Protein-protein interaction databases

STRINGi99287.STM1916.

Structurei

Secondary structure

1
129
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 114Combined sources
Helixi15 – 2814Combined sources
Beta strandi33 – 386Combined sources
Helixi39 – 468Combined sources
Beta strandi53 – 586Combined sources
Beta strandi61 – 633Combined sources
Helixi65 – 7410Combined sources
Turni76 – 805Combined sources
Beta strandi83 – 897Combined sources
Helixi92 – 1009Combined sources
Beta strandi104 – 1107Combined sources
Helixi113 – 12715Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CHEX-ray1.80A2-129[»]
2CHFX-ray1.80A2-129[»]
2CHYX-ray2.70A2-129[»]
2FKAX-ray2.00A1-129[»]
2FLKX-ray2.10A1-129[»]
2FLWX-ray2.00A1-129[»]
2FMFX-ray2.00A1-129[»]
2FMHX-ray2.00A1-129[»]
2FMIX-ray2.30A1-129[»]
2FMKX-ray2.00A1-129[»]
2PL9X-ray2.60A/B/C2-129[»]
2PMCX-ray2.69A/B/C/D2-129[»]
ProteinModelPortaliP0A2D5.
SMRiP0A2D5. Positions 2-129.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A2D5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 124118Response regulatoryPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 response regulatory domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0784.
HOGENOMiHOG000034820.
KOiK03413.
OMAiMLQSGAF.
OrthoDBiEOG6PKFC7.
PhylomeDBiP0A2D5.

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.

P0A2D5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADKELKFLV VDDFSTMRRI VRNLLKELGF NNVEEAEDGV DALNKLQAGG
60 70 80 90 100
FGFIISDWNM PNMDGLELLK TIRADSAMSA LPVLMVTAEA KKENIIAAAQ
110 120
AGASGYVVKP FTAATLEEKL NKIFEKLGM
Length:129
Mass (Da):14,125
Last modified:January 23, 2007 - v2
Checksum:iA0B4712E18626207
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12131 Genomic DNA. Translation: AAA27037.1.
AE006468 Genomic DNA. Translation: AAL20832.1.
PIRiA23567. QREBCY.
RefSeqiNP_460873.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL20832; AAL20832; STM1916.
GeneIDi1253437.
KEGGistm:STM1916.
PATRICi32382387. VBISalEnt20916_2032.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12131 Genomic DNA. Translation: AAA27037.1.
AE006468 Genomic DNA. Translation: AAL20832.1.
PIRiA23567. QREBCY.
RefSeqiNP_460873.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CHEX-ray1.80A2-129[»]
2CHFX-ray1.80A2-129[»]
2CHYX-ray2.70A2-129[»]
2FKAX-ray2.00A1-129[»]
2FLKX-ray2.10A1-129[»]
2FLWX-ray2.00A1-129[»]
2FMFX-ray2.00A1-129[»]
2FMHX-ray2.00A1-129[»]
2FMIX-ray2.30A1-129[»]
2FMKX-ray2.00A1-129[»]
2PL9X-ray2.60A/B/C2-129[»]
2PMCX-ray2.69A/B/C/D2-129[»]
ProteinModelPortaliP0A2D5.
SMRiP0A2D5. Positions 2-129.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi99287.STM1916.

Proteomic databases

PaxDbiP0A2D5.
PRIDEiP0A2D5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL20832; AAL20832; STM1916.
GeneIDi1253437.
KEGGistm:STM1916.
PATRICi32382387. VBISalEnt20916_2032.

Phylogenomic databases

eggNOGiCOG0784.
HOGENOMiHOG000034820.
KOiK03413.
OMAiMLQSGAF.
OrthoDBiEOG6PKFC7.
PhylomeDBiP0A2D5.

Enzyme and pathway databases

BioCyciSENT99287:GCTI-1928-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A2D5.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiCHEY_SALTY
AccessioniPrimary (citable) accession number: P0A2D5
Secondary accession number(s): P06657
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: January 7, 2015
This is version 82 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, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.