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P0A2D5

- CHEY_SALTY

UniProt

P0A2D5 - CHEY_SALTY

Protein

Chemotaxis protein CheY

Gene

cheY

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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 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
    2. phosphorelay response regulator activity Source: InterPro

    GO - Biological processi

    1. archaeal or bacterial-type flagellum-dependent cell motility Source: UniProtKB-KW
    2. chemotaxis Source: UniProtKB-KW

    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. cytoplasm Source: UniProtKB-SubCell

    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-aspartylphosphate2 PublicationsPROSITE-ProRule annotation
    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 – 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.
    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.
    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]FASTAAdd to Basket

    « 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.
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M12131 Genomic DNA. Translation: AAA27037.1 .
    AE006468 Genomic DNA. Translation: AAL20832.1 .
    PIRi A23567. QREBCY.
    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...
    MobiDBi 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

    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: October 1, 2014
    This is version 79 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