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Q9X006

- CHEC_THEMA

UniProt

Q9X006 - CHEC_THEMA

Protein

CheY-P phosphatase CheC

Gene

cheC

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 68 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    Functioni

    Involved in restoring normal CheY-P levels by dephosphorylating CheY-P. Inhibits CheD by incorporating in its fold a structural motif that mimics a CheD substrate recognition site to bait and inactivate it.

    GO - Molecular functioni

    1. hydrolase activity Source: UniProtKB-KW

    GO - Biological processi

    1. chemotaxis Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Chemotaxis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    CheY-P phosphatase CheC (EC:3.-.-.-)
    Gene namesi
    Name:cheC
    Ordered Locus Names:TM_0904
    OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
    Taxonomic identifieri243274 [NCBI]
    Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
    ProteomesiUP000008183: Chromosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi13 – 131E → S: Loss of activity, in absence of CheD; in presence of CheD, activity greater than wild-type CheC alone. Loss of activity, in absence of CheD; when associated with S-112. In presence of CheD, reduced activity but exceeds activity of CheC alone; when associated with S-112. 1 Publication
    Mutagenesisi16 – 161N → S: Loss of activity, in absence of CheD; in presence of CheD, activity greater than wild-type CheC alone. Loss of activity, in absence of CheD; when associated with S-115. In presence of CheD, almost no activity; when associated with S-115. 1 Publication
    Mutagenesisi112 – 1121E → S: Loss of activity, in absence of CheD; in presence of CheD, activity greater than wild-type CheC alone. Loss of activity, in absence of CheD; when associated with S-13. In presence of CheD, reduced activity but exceeds activity of CheC alone; when associated with S-13. 1 Publication
    Mutagenesisi115 – 1151N → S: Loss of activity, in absence of CheD; in presence of CheD, reduced activity. Loss of activity, in absence of CheD; when associated with S-16. In presence of CheD, almost no activity; when associated with S-16. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 205205CheY-P phosphatase CheCPRO_0000250997Add
    BLAST

    Interactioni

    Subunit structurei

    Heterodimer with CheD. The CheC-CheD heterodimer interacts with phosphorylated CheY. The CheC-CheD dimer has higher phosphatase activity than CheC alone.1 Publication

    Protein-protein interaction databases

    STRINGi243274.TM0904.

    Structurei

    Secondary structure

    1
    205
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi5 – 3026
    Beta strandi34 – 374
    Beta strandi41 – 455
    Helixi46 – 527
    Beta strandi59 – 7113
    Beta strandi73 – 797
    Helixi81 – 9212
    Helixi104 – 12926
    Beta strandi133 – 1353
    Beta strandi139 – 1446
    Helixi145 – 15713
    Beta strandi164 – 17411
    Beta strandi177 – 1793
    Beta strandi181 – 1899
    Helixi193 – 1997

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1XKRX-ray1.75A1-205[»]
    2F9ZX-ray2.40A/B1-205[»]
    ProteinModelPortaliQ9X006.
    SMRiQ9X006. Positions 1-204.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9X006.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the CheC family.Curated

    Phylogenomic databases

    eggNOGiCOG1776.
    KOiK03410.
    OMAiAPGNMFF.
    OrthoDBiEOG6ZPSZN.

    Family and domain databases

    Gene3Di3.40.1550.10. 1 hit.
    InterProiIPR007597. CheC.
    IPR028976. CheC-like_dom.
    [Graphical view]
    PfamiPF04509. CheC. 2 hits.
    [Graphical view]
    SUPFAMiSSF103039. SSF103039. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9X006-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKISERQKDL LKEIGNIGAG NAATAISYMI NKKVEISVPN VEIVPISKVI    50
    FIAKDPEEIV VGVKMPVTGD IEGSVLLIMG TTVVKKILEI LTGRAPDNLL 100
    NLDEFSASAL REIGNIMCGT YVSALADFLG FKIDTLPPQL VIDMISAIFA 150
    EASIEELEDN SEDQIVFVET LLKVEEEEEP LTSYMMMIPK PGYLVKIFER 200
    MGIQE 205
    Length:205
    Mass (Da):22,549
    Last modified:November 1, 1999 - v1
    Checksum:i0FF88D0E26A927B7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000512 Genomic DNA. Translation: AAD35985.1.
    PIRiG72318.
    RefSeqiNP_228712.1. NC_000853.1.
    YP_007977256.1. NC_021214.1.
    YP_008990126.1. NC_023151.1.

    Genome annotation databases

    EnsemblBacteriaiAAD35985; AAD35985; TM_0904.
    GeneIDi898578.
    KEGGitma:TM0904.
    tmi:THEMA_00115.
    tmm:Tmari_0906.
    PATRICi23936739. VBITheMar51294_0918.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000512 Genomic DNA. Translation: AAD35985.1 .
    PIRi G72318.
    RefSeqi NP_228712.1. NC_000853.1.
    YP_007977256.1. NC_021214.1.
    YP_008990126.1. NC_023151.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1XKR X-ray 1.75 A 1-205 [» ]
    2F9Z X-ray 2.40 A/B 1-205 [» ]
    ProteinModelPortali Q9X006.
    SMRi Q9X006. Positions 1-204.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 243274.TM0904.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAD35985 ; AAD35985 ; TM_0904 .
    GeneIDi 898578.
    KEGGi tma:TM0904.
    tmi:THEMA_00115.
    tmm:Tmari_0906.
    PATRICi 23936739. VBITheMar51294_0918.

    Phylogenomic databases

    eggNOGi COG1776.
    KOi K03410.
    OMAi APGNMFF.
    OrthoDBi EOG6ZPSZN.

    Miscellaneous databases

    EvolutionaryTracei Q9X006.

    Family and domain databases

    Gene3Di 3.40.1550.10. 1 hit.
    InterProi IPR007597. CheC.
    IPR028976. CheC-like_dom.
    [Graphical view ]
    Pfami PF04509. CheC. 2 hits.
    [Graphical view ]
    SUPFAMi SSF103039. SSF103039. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
    2. "Structure and function of an unusual family of protein phosphatases: the bacterial chemotaxis proteins CheC and CheX."
      Park S.-Y., Chao X., Gonzalez-Bonet G., Beel B.D., Bilwes A.M., Crane B.R.
      Mol. Cell 16:563-574(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), MUTAGENESIS OF GLU-13; ASN-16; GLU-112 AND ASN-115.
    3. "A receptor-modifying deamidase in complex with a signaling phosphatase reveals reciprocal regulation."
      Chao X., Muff T.J., Park S.-Y., Zhang S., Pollard A.M., Ordal G.W., Bilwes A.M., Crane B.R.
      Cell 124:561-571(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH CHED.

    Entry informationi

    Entry nameiCHEC_THEMA
    AccessioniPrimary (citable) accession number: Q9X006
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 3, 2006
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 68 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