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Q56312

- CHEY_THEMA

UniProt

Q56312 - CHEY_THEMA

Protein

Chemotaxis protein CheY

Gene

cheY

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheY seems to regulate the clockwise (CW) rotation By similarity.By similarity

    Cofactori

    Binds 1 magnesium ion per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi9 – 91Magnesium
    Metal bindingi10 – 101Magnesium
    Metal bindingi54 – 541Magnesium
    Metal bindingi56 – 561Magnesium; via carbonyl oxygen

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. phosphorelay response regulator activity Source: InterPro
    3. protein binding Source: UniProtKB

    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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Chemotaxis protein CheY
    Gene namesi
    Name:cheY
    Ordered Locus Names:TM_0700
    OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
    Taxonomic identifieri243274 [NCBI]
    Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
    ProteomesiUP000008183: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 120120Chemotaxis protein CheYPRO_0000081055Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei54 – 5414-aspartylphosphate1 PublicationPROSITE-ProRule annotation

    Post-translational modificationi

    Phosphorylated by CheA.By similarity

    Keywords - PTMi

    Phosphoprotein

    Interactioni

    Protein-protein interaction databases

    IntActiQ56312. 1 interaction.
    STRINGi243274.TM0700.

    Structurei

    Secondary structure

    1
    120
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 85
    Helixi12 – 2413
    Beta strandi28 – 358
    Helixi36 – 4611
    Beta strandi49 – 535
    Beta strandi58 – 603
    Helixi62 – 7211
    Beta strandi78 – 836
    Helixi87 – 9610
    Beta strandi99 – 1057
    Helixi108 – 11710

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1TMYX-ray1.90A1-120[»]
    1U0SX-ray1.90Y2-119[»]
    2LLENMR-A1-103[»]
    2TMYX-ray2.30A1-120[»]
    3TMYX-ray2.20A/B1-120[»]
    4IGAX-ray1.73A1-120[»]
    4TMYX-ray2.80A/B1-120[»]
    ProteinModelPortaliQ56312.
    SMRiQ56312. Positions 2-119.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ56312.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 119119Response regulatoryPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 response regulatory domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0784.
    KOiK03413.
    OMAiITESCKA.
    OrthoDBiEOG6PKFC7.

    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.

    Q56312-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGKRVLIVDD AAFMRMMLKD IITKAGYEVA GEATNGREAV EKYKELKPDI    50
    VTMDITMPEM NGIDAIKEIM KIDPNAKIIV CSAMGQQAMV IEAIKAGAKD 100
    FIVKPFQPSR VVEALNKVSK 120
    Length:120
    Mass (Da):13,217
    Last modified:November 1, 1996 - v1
    Checksum:i195AC95641264E63
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U30501 Genomic DNA. Translation: AAA96389.1.
    AE000512 Genomic DNA. Translation: AAD35782.1.
    PIRiB72346.
    RefSeqiNP_228509.1. NC_000853.1.
    YP_007977050.1. NC_021214.1.
    YP_008990331.1. NC_023151.1.

    Genome annotation databases

    EnsemblBacteriaiAAD35782; AAD35782; TM_0700.
    GeneIDi898367.
    KEGGitma:TM0700.
    tmi:THEMA_01165.
    tmm:Tmari_0700.
    PATRICi23936318. VBITheMar51294_0712.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U30501 Genomic DNA. Translation: AAA96389.1 .
    AE000512 Genomic DNA. Translation: AAD35782.1 .
    PIRi B72346.
    RefSeqi NP_228509.1. NC_000853.1.
    YP_007977050.1. NC_021214.1.
    YP_008990331.1. NC_023151.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1TMY X-ray 1.90 A 1-120 [» ]
    1U0S X-ray 1.90 Y 2-119 [» ]
    2LLE NMR - A 1-103 [» ]
    2TMY X-ray 2.30 A 1-120 [» ]
    3TMY X-ray 2.20 A/B 1-120 [» ]
    4IGA X-ray 1.73 A 1-120 [» ]
    4TMY X-ray 2.80 A/B 1-120 [» ]
    ProteinModelPortali Q56312.
    SMRi Q56312. Positions 2-119.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q56312. 1 interaction.
    STRINGi 243274.TM0700.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAD35782 ; AAD35782 ; TM_0700 .
    GeneIDi 898367.
    KEGGi tma:TM0700.
    tmi:THEMA_01165.
    tmm:Tmari_0700.
    PATRICi 23936318. VBITheMar51294_0712.

    Phylogenomic databases

    eggNOGi COG0784.
    KOi K03413.
    OMAi ITESCKA.
    OrthoDBi EOG6PKFC7.

    Miscellaneous databases

    EvolutionaryTracei Q56312.

    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. "Thermostable chemotaxis proteins from the hyperthermophilic bacterium Thermotoga maritima."
      Swanson R.V., Sanna M.G., Simon M.I.
      J. Bacteriol. 178:484-489(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
    3. "Crystal structures of CheY from Thermotoga maritima do not support conventional explanations for the structural basis of enhanced thermostability."
      Usher K.C., de la Cruz A.F.A., Dahlquist F.W., Swanson R.V., Simon M.I., Remington S.J.
      Protein Sci. 7:403-412(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), PHOSPHORYLATION AT ASP-54.

    Entry informationi

    Entry nameiCHEY_THEMA
    AccessioniPrimary (citable) accession number: Q56312
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 108 of the entry and version 1 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