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P0A2D5

- CHEY_SALTY

UniProt

P0A2D5 - CHEY_SALTY

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Protein
Chemotaxis protein CheY
Gene
cheY, STM1916
Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
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. Shows autophosphatase activity which is enhanced by CheZ.

Cofactori

Binds 1 magnesium ion per subunit.

Sites

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

GO - Molecular functioni

  1. metal ion bindingInferred from electronic annotationi Source: UniProtKB-KW
  2. phosphorelay response regulator activityInferred from electronic annotationi Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. archaeal or bacterial-type flagellum-dependent cell motilityInferred from electronic annotationi Source: UniProtKB-KW
  2. chemotaxisInferred from electronic annotationi Source: UniProtKB-KW
  1. phosphorelay response regulator activityInferred from electronic annotationi Source: InterPro
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: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. cytoplasmInferred from electronic annotationi Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
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 identifier
Initiator methioninei1 – 11Removed
Chaini2 – 129128Chemotaxis protein CheY
PRO_0000081045

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Modified residuei57 – 5714-aspartylphosphate
Modified residuei92 – 921N6-acetyllysine By similarity
Modified residuei109 – 1091N6-acetyllysine By 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.4 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP0A2D5.
PRIDEiP0A2D5.

Interactioni

Subunit structurei

Interacts (phosphorylated CheY) with CheZ (via C-terminus).1 Publication

Protein-protein interaction databases

STRINGi99287.STM1916.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Beta strandi8 – 114
Helixi15 – 2814
Beta strandi33 – 386
Helixi39 – 468
Beta strandi53 – 586
Beta strandi61 – 633
Helixi65 – 7410
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
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.

Miscellaneous databases

EvolutionaryTraceiP0A2D5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Domaini7 – 124118Response regulatory

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0784.
HOGENOMiHOG000034820.
KOiK03413.
OMAiGHDEELH.
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]FASTA

« Hide

MADKELKFLV VDDFSTMRRI VRNLLKELGF NNVEEAEDGV DALNKLQAGG    50
FGFIISDWNM PNMDGLELLK TIRADSAMSA LPVLMVTAEA KKENIIAAAQ 100
AGASGYVVKP FTAATLEEKL NKIFEKLGM 129
Length:129
Mass (Da):14,125
Last modified:January 23, 2007 - v2
Checksum:iA0B4712E18626207
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M12131 Genomic DNA. Translation: AAA27037.1.
AE006468 Genomic DNA. Translation: AAL20832.1.
PIRiQREBCY. A23567.
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:
EMBL
GenBank
DDBJ
Links Updated
M12131 Genomic DNA. Translation: AAA27037.1 .
AE006468 Genomic DNA. Translation: AAL20832.1 .
PIRi QREBCY. A23567.
RefSeqi NP_460873.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 1-129 [» ]
2FLK X-ray 2.10 A 1-129 [» ]
2FLW X-ray 2.00 A 1-129 [» ]
2FMF X-ray 2.00 A 1-129 [» ]
2FMH X-ray 2.00 A 1-129 [» ]
2FMI X-ray 2.30 A 1-129 [» ]
2FMK X-ray 2.00 A 1-129 [» ]
2PL9 X-ray 2.60 A/B/C 2-129 [» ]
2PMC X-ray 2.69 A/B/C/D 2-129 [» ]
ProteinModelPortali P0A2D5.
SMRi P0A2D5. Positions 2-129.
ModBasei Search...

Protein-protein interaction databases

STRINGi 99287.STM1916.

Proteomic databases

PaxDbi P0A2D5.
PRIDEi P0A2D5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAL20832 ; AAL20832 ; STM1916 .
GeneIDi 1253437.
KEGGi stm:STM1916.
PATRICi 32382387. VBISalEnt20916_2032.

Phylogenomic databases

eggNOGi COG0784.
HOGENOMi HOG000034820.
KOi K03413.
OMAi GHDEELH.
OrthoDBi EOG6PKFC7.
PhylomeDBi P0A2D5.

Enzyme and pathway databases

BioCyci SENT99287:GCTI-1928-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0A2D5.

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' publicationsDownload
  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.

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: July 9, 2014
This is version 78 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. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

External Data

Dasty 3

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