RegulonDB RegulonDB 10.9: Gene Form
   

cheZ gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

flhB cheZ cheY flhA FlhDC FlhDC flhBp flhBp

Gene      
Name: cheZ    Texpresso search in the literature
Synonym(s): ECK1882, EG10151, b1881
Genome position(nucleotides): 1966393 <-- 1967037 Genome Browser
Strand: reverse
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
53.49
External database links:  
ASAP:
ABE-0006278
CGSC:
923
ECHOBASE:
EB0149
ECOLIHUB:
cheZ
OU-MICROARRAY:
b1881
STRING:
511145.b1881
COLOMBOS: cheZ


Product      
Name: chemotaxis protein CheZ
Synonym(s): CheZ
Sequence: Get amino acid sequence Fasta Format
Cellular location: cytosol,inner membrane,cell projection
Molecular weight: 23.976
Isoelectric point: 4.202
Motif(s):
 
Type Positions Sequence
17 -> 214 IIARIGSLTRMLRDSLRELGLDQAIAEAAEAIPDARDRLYYVVQMTAQAAERALNSVEASQPHQDQMEKSAKALTQRWDDWFADPIDLADARELVTDTRQFLADVPAHTSFTNAQLLEIMMAQDFQDLTGQVIKRMMDVIQEIERQLLMVLLENIPEQESRPKRENQSLLNGPQVDTSKAGVVASQDQVDDLLDSLGF
65 -> 65 A
130 -> 130 A
24 -> 24 L
152 -> 152 M

 

Classification:
Multifun Terms (GenProtEC)  
  2 - information transfer --> 2.3 - protein related --> 2.3.3 - posttranslational modification
  5 - cell processes --> 5.3 - motility, chemotaxis, energytaxis (aerotaxis, redoxtaxis etc)
Gene Ontology Terms (GO)  
cellular_component GO:0098561 - methyl accepting chemotaxis protein complex
GO:0005737 - cytoplasm
GO:0005829 - cytosol
GO:0005886 - plasma membrane
GO:0009288 - bacterial-type flagellum
molecular_function GO:0051219 - phosphoprotein binding
GO:0003824 - catalytic activity
GO:0005515 - protein binding
GO:0016787 - hydrolase activity
GO:0004721 - phosphoprotein phosphatase activity
GO:0042802 - identical protein binding
GO:0042803 - protein homodimerization activity
biological_process GO:0006470 - protein dephosphorylation
GO:0006935 - chemotaxis
GO:0050920 - regulation of chemotaxis
GO:0071978 - bacterial-type flagellum-dependent swarming motility
GO:0097588 - archaeal or bacterial-type flagellum-dependent cell motility
Reference(s): [1] Blat Y., et al., 1994
[2] Blat Y., et al., 1996
[3] Blat Y., et al., 1996
[4] Blat Y., et al., 1996
[5] Bren A., et al., 1996
[6] Cantwell BJ., et al., 2003
[7] Hao S., et al., 2009
[8] Hess JF., et al., 1987
[9] McNamara BP., et al., 1997
[10] Sanna MG., et al., 1996
[11] Sanna MG., et al., 1995
[12] Wang H., et al., 1996
[13] van Albada SB., et al., 2009
External database links:  
DIP:
DIP-9275N
ECOCYC:
CHEZ-MONOMER
ECOLIWIKI:
b1881
INTERPRO:
IPR007439
MODBASE:
P0A9H9
PDB:
1KMI
PFAM:
PF04344
PRIDE:
P0A9H9
PRODB:
PRO_000022282
REFSEQ:
NP_416395
SMR:
P0A9H9
UNIPROT:
P0A9H9


Operon      
Name: tar-tap-cheRBYZ         
Operon arrangement:
Transcription unit        Promoter
tar-tap-cheRBYZ


Transcriptional Regulation      
Display Regulation             
Activated by: FNR


Elements in the selected gene context region unrelated to any object in RegulonDB      

  Type Name Post Left Post Right Strand Notes Evidence (Confirmed, Strong, Weak) References


Reference(s)    

 [1] Blat Y., Eisenbach M., 1994, Phosphorylation-dependent binding of the chemotaxis signal molecule CheY to its phosphatase, CheZ., Biochemistry 33(4):902-6

 [2] Blat Y., Eisenbach M., 1996, Oligomerization of the phosphatase CheZ upon interaction with the phosphorylated form of CheY. The signal protein of bacterial chemotaxis., J Biol Chem 271(2):1226-31

 [3] Blat Y., Eisenbach M., 1996, Mutants with defective phosphatase activity show no phosphorylation-dependent oligomerization of CheZ. The phosphatase of bacterial chemotaxis., J Biol Chem 271(2):1232-6

 [4] Blat Y., Eisenbach M., 1996, Conserved C-terminus of the phosphatase CheZ is a binding domain for the chemotactic response regulator CheY., Biochemistry 35(18):5679-83

 [5] Bren A., Welch M., Blat Y., Eisenbach M., 1996, Signal termination in bacterial chemotaxis: CheZ mediates dephosphorylation of free rather than switch-bound CheY., Proc Natl Acad Sci U S A 93(19):10090-3

 [6] Cantwell BJ., Draheim RR., Weart RB., Nguyen C., Stewart RC., Manson MD., 2003, CheZ phosphatase localizes to chemoreceptor patches via CheA-short., J Bacteriol 185(7):2354-61

 [7] Hao S., Hamel D., Zhou H., Dahlquist FW., 2009, Structural basis for the localization of the chemotaxis phosphatase CheZ by CheAS., J Bacteriol 191(18):5842-4

 [8] Hess JF., Oosawa K., Matsumura P., Simon MI., 1987, Protein phosphorylation is involved in bacterial chemotaxis., Proc Natl Acad Sci U S A 84(21):7609-13

 [9] McNamara BP., Wolfe AJ., 1997, Coexpression of the long and short forms of CheA, the chemotaxis histidine kinase, by members of the family Enterobacteriaceae., J Bacteriol 179(5):1813-8

 [10] Sanna MG., Simon MI., 1996, Isolation and in vitro characterization of CheZ suppressors for the Escherichia coli chemotactic response regulator mutant CheYN23D., J Biol Chem 271(13):7357-61

 [11] Sanna MG., Swanson RV., Bourret RB., Simon MI., 1995, Mutations in the chemotactic response regulator, CheY, that confer resistance to the phosphatase activity of CheZ., Mol Microbiol 15(6):1069-79

 [12] Wang H., Matsumura P., 1996, Characterization of the CheAS/CheZ complex: a specific interaction resulting in enhanced dephosphorylating activity on CheY-phosphate., Mol Microbiol 19(4):695-703

 [13] van Albada SB., Ten Wolde PR., 2009, Differential affinity and catalytic activity of CheZ in E. coli chemotaxis., PLoS Comput Biol 5(5):e1000378


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