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P0A9H9

- CHEZ_ECOLI

UniProt

P0A9H9 - CHEZ_ECOLI

Protein

Protein phosphatase CheZ

Gene

cheZ

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 1 (01 Apr 1988)
      Previous versions | rss
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    Functioni

    Plays an important role in bacterial chemotaxis signal transduction pathway by accelerating the dephosphorylation of phosphorylated CheY (CheY-P).2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei147 – 1471Enhances dephosphorylation of CheY-P

    GO - Molecular functioni

    1. phosphoprotein phosphatase activity Source: EcoCyc
    2. protein binding Source: IntAct

    GO - Biological processi

    1. bacterial-type flagellum-dependent swimming motility Source: EcoCyc
    2. chemotaxis Source: UniProtKB-KW
    3. dephosphorylation Source: GOC
    4. regulation of chemotaxis Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Biological processi

    Chemotaxis, Flagellar rotation

    Enzyme and pathway databases

    BioCyciEcoCyc:CHEZ-MONOMER.
    ECOL316407:JW1870-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein phosphatase CheZ (EC:3.1.3.-)
    Alternative name(s):
    Chemotaxis protein CheZ
    Gene namesi
    Name:cheZ
    Ordered Locus Names:b1881, JW1870
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10151. cheZ.

    Subcellular locationi

    Cytoplasm 1 Publication
    Note: Colocalizes with CheA chemoreceptor patches near the cell poles, which requires CheA(short).

    GO - Cellular componenti

    1. bacterial-type flagellum Source: InterPro
    2. cytosol Source: EcoCyc
    3. plasma membrane Source: EcoCyc

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi21 – 211I → T: Gain of function, increased counterclockwise rotation of flagella. 1 Publication
    Mutagenesisi65 – 651A → V: Loss of function, fails to oligomerize. 1 Publication
    Mutagenesisi90 – 901L → S: Loss of localization to the cell pole. Fails to oligomerize. 2 Publications
    Mutagenesisi94 – 941W → R: Loss of localization to the cell pole. 1 Publication
    Mutagenesisi117 – 1171F → S: Loss of localization to the cell pole. 2 Publications
    Mutagenesisi143 – 1431D → G: Loss of function. Fails to oligomerize. 1 Publication
    Mutagenesisi147 – 1471Q → A: Severely diminished function, exclusive clockwise flagellar rotation. 1 Publication
    Mutagenesisi188 – 1881G → E: Diminished ability to stimulate dephosphorylation of CheY-P. 1 Publication
    Mutagenesisi205 – 2051V → E: Severely impairs the interaction the interaction with CheY-P. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 214214Protein phosphatase CheZPRO_0000089641Add
    BLAST

    Proteomic databases

    PaxDbiP0A9H9.
    PRIDEiP0A9H9.

    2D gel databases

    SWISS-2DPAGEP0A9H9.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A9H9.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with CheA isoform CheA(short). Interacts (via C-terminus) with phosphorylated CheY (CheY-P).4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    cheAP073633EBI-546726,EBI-1026773
    cheYP0AE673EBI-546726,EBI-546693

    Protein-protein interaction databases

    DIPiDIP-47931N.
    IntActiP0A9H9. 22 interactions.
    MINTiMINT-1264225.
    STRINGi511145.b1881.

    Structurei

    Secondary structure

    1
    214
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi14 – 3522
    Helixi37 – 437
    Turni44 – 474
    Helixi48 – 547
    Turni55 – 573
    Helixi58 – 647
    Turni65 – 673
    Helixi68 – 9730
    Helixi104 – 13835
    Helixi141 – 16121
    Turni162 – 1676
    Helixi204 – 2129

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1KMIX-ray2.90Z1-214[»]
    ProteinModelPortaliP0A9H9.
    SMRiP0A9H9. Positions 5-213.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A9H9.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the CheZ family.Curated

    Phylogenomic databases

    eggNOGiCOG3143.
    HOGENOMiHOG000254724.
    KOiK03414.
    OMAiGPQIHAD.
    OrthoDBiEOG6Z9B15.
    PhylomeDBiP0A9H9.

    Family and domain databases

    InterProiIPR007439. Chemotax_Pase_CheZ.
    [Graphical view]
    PfamiPF04344. CheZ. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002884. CheZ. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P0A9H9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMQPSIKPAD EHSAGDIIAR IGSLTRMLRD SLRELGLDQA IAEAAEAIPD    50
    ARDRLYYVVQ MTAQAAERAL NSVEASQPHQ DQMEKSAKAL TQRWDDWFAD 100
    PIDLADAREL VTDTRQFLAD VPAHTSFTNA QLLEIMMAQD FQDLTGQVIK 150
    RMMDVIQEIE RQLLMVLLEN IPEQESRPKR ENQSLLNGPQ VDTSKAGVVA 200
    SQDQVDDLLD SLGF 214
    Length:214
    Mass (Da):23,976
    Last modified:April 1, 1988 - v1
    Checksum:i42308F5AC0685D27
    GO

    Sequence cautioni

    The sequence AAA23571.1 differs from that shown. Reason:

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti119 – 1191A → P in AAA23571. (PubMed:3510184)Curated
    Sequence conflicti130 – 1301A → G in AAA23571. (PubMed:3510184)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M13463 Genomic DNA. Translation: AAA23571.1. Sequence problems.
    U00096 Genomic DNA. Translation: AAC74951.1.
    AP009048 Genomic DNA. Translation: BAA15697.1.
    K02175 Genomic DNA. Translation: AAA23578.1.
    PIRiF25195. QRECCZ.
    RefSeqiNP_416395.1. NC_000913.3.
    YP_490143.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74951; AAC74951; b1881.
    BAA15697; BAA15697; BAA15697.
    GeneIDi12930560.
    946392.
    KEGGiecj:Y75_p1857.
    eco:b1881.
    PATRICi32119089. VBIEscCol129921_1962.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M13463 Genomic DNA. Translation: AAA23571.1 . Sequence problems.
    U00096 Genomic DNA. Translation: AAC74951.1 .
    AP009048 Genomic DNA. Translation: BAA15697.1 .
    K02175 Genomic DNA. Translation: AAA23578.1 .
    PIRi F25195. QRECCZ.
    RefSeqi NP_416395.1. NC_000913.3.
    YP_490143.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1KMI X-ray 2.90 Z 1-214 [» ]
    ProteinModelPortali P0A9H9.
    SMRi P0A9H9. Positions 5-213.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-47931N.
    IntActi P0A9H9. 22 interactions.
    MINTi MINT-1264225.
    STRINGi 511145.b1881.

    2D gel databases

    SWISS-2DPAGE P0A9H9.

    Proteomic databases

    PaxDbi P0A9H9.
    PRIDEi P0A9H9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC74951 ; AAC74951 ; b1881 .
    BAA15697 ; BAA15697 ; BAA15697 .
    GeneIDi 12930560.
    946392.
    KEGGi ecj:Y75_p1857.
    eco:b1881.
    PATRICi 32119089. VBIEscCol129921_1962.

    Organism-specific databases

    EchoBASEi EB0149.
    EcoGenei EG10151. cheZ.

    Phylogenomic databases

    eggNOGi COG3143.
    HOGENOMi HOG000254724.
    KOi K03414.
    OMAi GPQIHAD.
    OrthoDBi EOG6Z9B15.
    PhylomeDBi P0A9H9.

    Enzyme and pathway databases

    BioCyci EcoCyc:CHEZ-MONOMER.
    ECOL316407:JW1870-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0A9H9.
    PROi P0A9H9.

    Gene expression databases

    Genevestigatori P0A9H9.

    Family and domain databases

    InterProi IPR007439. Chemotax_Pase_CheZ.
    [Graphical view ]
    Pfami PF04344. CheZ. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002884. CheZ. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence corresponding to five chemotaxis genes in Escherichia coli."
      Mutoh N., Simon M.I.
      J. Bacteriol. 165:161-166(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "Overexpression and sequence of the Escherichia coli cheY gene and biochemical activities of the CheY protein."
      Matsumura P., Rydel J.J., Linzmeier R., Vacante D.
      J. Bacteriol. 160:36-41(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14.
    6. "Characterization of the CheAS/CheZ complex: a specific interaction resulting in enhanced dephosphorylating activity on CheY-phosphate."
      Wang H., Matsumura P.
      Mol. Microbiol. 19:695-703(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CHEA AND CHEY.
    7. "Escherichia coli proteome analysis using the gene-protein database."
      VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
      Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.
    8. "Isolation and characterization of nonchemotactic CheZ mutants of Escherichia coli."
      Boesch K.C., Silversmith R.E., Bourret R.B.
      J. Bacteriol. 182:3544-3552(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CHEY, MUTAGENESIS OF ALA-65; LEU-90; PHE-117; ASP-143; GLY-188 AND VAL-205.
    9. "CheZ phosphatase localizes to chemoreceptor patches via CheA-short."
      Cantwell B.J., Draheim R.R., Weart R.B., Nguyen C., Stewart R.C., Manson M.D.
      J. Bacteriol. 185:2354-2361(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-90; TRY-94 AND PHE-117.
    10. "Kinetic characterization of catalysis by the chemotaxis phosphatase CheZ. Modulation of activity by the phosphorylated CheY substrate."
      Silversmith R.E., Levin M.D., Schilling E., Bourret R.B.
      J. Biol. Chem. 283:756-765(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ILE-21, INTERACTION WITH CHEY.
    11. "Structure and catalytic mechanism of the E. coli chemotaxis phosphatase CheZ."
      Zhao R., Collins E.J., Bourret R.B., Silversmith R.E.
      Nat. Struct. Biol. 9:570-575(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH CHEY, SUBUNIT, MUTAGENESIS OF GLN-147.

    Entry informationi

    Entry nameiCHEZ_ECOLI
    AccessioniPrimary (citable) accession number: P0A9H9
    Secondary accession number(s): P07366
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: April 1, 1988
    Last modified: October 1, 2014
    This is version 74 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. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3