Protein phosphatase CheZ - Escherichia coli (strain K12)

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P0A9H9 (CHEZ_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 66. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Protein phosphatase CheZ
EC=3.1.3.-

Alternative name(s):
Chemotaxis protein CheZ

Gene names

Name:	cheZ
Ordered Locus Names:	b1881, JW1870

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	214 AA.
Sequence status	Complete.
Protein existence	Evidence 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:

Ontologies

Keywords
Biological process	Chemotaxis Flagellar rotation
Cellular component	Cytoplasm
Molecular function	Hydrolase Protein phosphatase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	bacterial-type flagellar swimming motility Inferred from mutant phenotype PubMed 3456269. Source: EcoCyc chemotaxis Inferred from electronic annotation. Source: UniProtKB-KW regulation of chemotaxis Inferred from electronic annotation. Source: InterPro
Cellular_component	bacterial-type flagellum Inferred from electronic annotation. Source: InterPro cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	phosphoprotein phosphatase activity Inferred from direct assay Ref.6. Source: EcoCyc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
cheA	P07363	3	EBI-546726,EBI-1026773
cheY	P0AE67	3	EBI-546726,EBI-546693

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 214

214

Protein phosphatase CheZ

PRO_0000089641

Sites

Site

147

Enhances dephosphorylation of CheY-P

Experimental info

Mutagenesis

I → T: Gain of function, increased counterclockwise rotation of flagella. Ref.10

Mutagenesis

A → V: Loss of function, fails to oligomerize. Ref.8

Mutagenesis

L → S: Loss of localization to the cell pole. Fails to oligomerize. Ref.8 Ref.9

Mutagenesis

W → R: Loss of localization to the cell pole. Ref.9

Mutagenesis

117

F → S: Loss of localization to the cell pole. Ref.8 Ref.9

Mutagenesis

143

D → G: Loss of function. Fails to oligomerize. Ref.8

Mutagenesis

147

Q → A: Severely diminished function, exclusive clockwise flagellar rotation. Ref.11

Mutagenesis

188

G → E: Diminished ability to stimulate dephosphorylation of CheY-P. Ref.8

Mutagenesis

205

V → E: Severely impairs the interaction the interaction with CheY-P. Ref.8

Sequence conflict

119

A → P in AAA23571. Ref.1

Sequence conflict

130

A → G in AAA23571. Ref.1

Secondary structure

214

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A9H9 [UniParc].

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

FASTA

214

23,976

        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' referencesShow '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. 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 277:1453-1474(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.

PIR

QRECCZ. F25195.

RefSeq

NP_416395.1. NC_000913.2.
YP_490143.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KMI	X-ray	2.90	Z	1-214	[»]

ProteinModelPortal

P0A9H9.

SMR

P0A9H9. Positions 5-213.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-47931N.

IntAct

P0A9H9. 20 interactions.

MINT

MINT-1264225.

STRING

511145.b1881.

2D gel databases

SWISS-2DPAGE

P0A9H9.

Proteomic databases

PaxDb

P0A9H9.

PRIDE

P0A9H9.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC74951; AAC74951; b1881.
BAA15697; BAA15697; BAA15697.

GeneID

12930560.
946392.

KEGG

ecj:Y75_p1857.
eco:b1881.

PATRIC

32119089. VBIEscCol129921_1962.

Organism-specific databases

EchoBASE

EB0149.

EcoGene

EG10151. cheZ.

Phylogenomic databases

eggNOG

COG3143.

HOGENOM

HOG000254724.

K03414.

OMA

EGPQIHA.

ProtClustDB

PRK11166.

Enzyme and pathway databases

BioCyc

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

Gene expression databases

Genevestigator

P0A9H9.

Family and domain databases

InterPro

IPR007439. Chemotax_Pase_CheZ.
[Graphical view]

Pfam

PF04344. CheZ. 1 hit.
[Graphical view]

PIRSF

PIRSF002884. CheZ. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P0A9H9.

Entry information

Entry name

CHEZ_ECOLI

Accession

Primary (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:	May 1, 2013
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents