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P0A9H9

- CHEZ_ECOLI

UniProt

P0A9H9 - CHEZ_ECOLI

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Protein
Protein phosphatase CheZ
Gene
cheZ, b1881, JW1870
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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

GO - Cellular componenti

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

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 CheZ
PRO_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

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.

Miscellaneous databases

EvolutionaryTraceiP0A9H9.

Family & Domainsi

Sequence similaritiesi

Belongs to the CheZ family.

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:

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti119 – 1191A → P in AAA23571. 1 Publication
Sequence conflicti130 – 1301A → G in AAA23571. 1 Publication

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

« Hide 'large scale' publications
  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: June 11, 2014
This is version 73 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

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