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P0A9H9 (CHEZ_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein phosphatase CheZ

EC=3.1.3.-
Alternative name(s):
Chemotaxis protein CheZ
Gene names
Name:cheZ
Ordered Locus Names:b1881, JW1870
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length214 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays an important role in bacterial chemotaxis signal transduction pathway by accelerating the dephosphorylation of phosphorylated CheY (CheY-P). Ref.6 Ref.8

Subunit structure

Homodimer. Interacts with CheA isoform CheA(short) Interacts (via C-terminus) with phosphorylated CheY (CheY-P). Ref.6 Ref.8 Ref.10 Ref.11

Subcellular location

Cytoplasm. Note: Colocalizes with CheA chemoreceptor patches near the cell poles, which requires CheA(short). Ref.9

Sequence similarities

Belongs to the CheZ family.

Sequence caution

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

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 214214Protein phosphatase CheZ
PRO_0000089641

Sites

Site1471Enhances dephosphorylation of CheY-P

Experimental info

Mutagenesis211I → T: Gain of function, increased counterclockwise rotation of flagella. Ref.10
Mutagenesis651A → V: Loss of function, fails to oligomerize. Ref.8
Mutagenesis901L → S: Loss of localization to the cell pole. Fails to oligomerize. Ref.8 Ref.9
Mutagenesis941W → R: Loss of localization to the cell pole. Ref.9
Mutagenesis1171F → S: Loss of localization to the cell pole. Ref.8 Ref.9
Mutagenesis1431D → G: Loss of function. Fails to oligomerize. Ref.8
Mutagenesis1471Q → A: Severely diminished function, exclusive clockwise flagellar rotation. Ref.11
Mutagenesis1881G → E: Diminished ability to stimulate dephosphorylation of CheY-P. Ref.8
Mutagenesis2051V → E: Severely impairs the interaction the interaction with CheY-P. Ref.8
Sequence conflict1191A → P in AAA23571. Ref.1
Sequence conflict1301A → G in AAA23571. Ref.1

Secondary structure

.................. 214
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A9H9 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: 42308F5AC0685D27

FASTA21423,976
        10         20         30         40         50         60 
MMQPSIKPAD EHSAGDIIAR IGSLTRMLRD SLRELGLDQA IAEAAEAIPD ARDRLYYVVQ 

        70         80         90        100        110        120 
MTAQAAERAL NSVEASQPHQ DQMEKSAKAL TQRWDDWFAD PIDLADAREL VTDTRQFLAD 

       130        140        150        160        170        180 
VPAHTSFTNA QLLEIMMAQD FQDLTGQVIK RMMDVIQEIE RQLLMVLLEN IPEQESRPKR 

       190        200        210 
ENQSLLNGPQ VDTSKAGVVA SQDQVDDLLD SLGF 

« Hide

References

« Hide 'large scale' references
[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]"A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map."
Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S. expand/collapse author list , Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:379-392(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRQRECCZ. F25195.
RefSeqNP_416395.1. NC_000913.3.
YP_490143.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KMIX-ray2.90Z1-214[»]
ProteinModelPortalP0A9H9.
SMRP0A9H9. Positions 5-213.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-47931N.
IntActP0A9H9. 22 interactions.
MINTMINT-1264225.
STRING511145.b1881.

2D gel databases

SWISS-2DPAGEP0A9H9.

Proteomic databases

PaxDbP0A9H9.
PRIDEP0A9H9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74951; AAC74951; b1881.
BAA15697; BAA15697; BAA15697.
GeneID12930560.
946392.
KEGGecj:Y75_p1857.
eco:b1881.
PATRIC32119089. VBIEscCol129921_1962.

Organism-specific databases

EchoBASEEB0149.
EcoGeneEG10151. cheZ.

Phylogenomic databases

eggNOGCOG3143.
HOGENOMHOG000254724.
KOK03414.
OMAGPQIHAD.
OrthoDBEOG6Z9B15.
PhylomeDBP0A9H9.
ProtClustDBPRK11166.

Enzyme and pathway databases

BioCycEcoCyc:CHEZ-MONOMER.
ECOL316407:JW1870-MONOMER.

Gene expression databases

GenevestigatorP0A9H9.

Family and domain databases

InterProIPR007439. Chemotax_Pase_CheZ.
[Graphical view]
PfamPF04344. CheZ. 1 hit.
[Graphical view]
PIRSFPIRSF002884. CheZ. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP0A9H9.
PROP0A9H9.

Entry information

Entry nameCHEZ_ECOLI
AccessionPrimary (citable) accession number: P0A9H9
Secondary accession number(s): P07366
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: April 16, 2014
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene