RegulonDB

RegulonDB RegulonDB 11.1: Gene Form

cheZ gene in Escherichia coli K-12 genome

Gene local context to scale (view description)

Gene
Name:	cheZ
Synonym(s):	ECK1882, EG10151, b1881
Genome position(nucleotides):	1966393 <-- 1967037
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	Comment
	17 -> 214	IIARIGSLTRMLRDSLRELGLDQAIAEAAEAIPDARDRLYYVVQMTAQAAERALNSVEASQPHQDQMEKSAKALTQRWDDWFADPIDLADARELVTDTRQFLADVPAHTSFTNAQLLEIMMAQDFQDLTGQVIKRMMDVIQEIERQLLMVLLENIPEQESRPKRENQSLLNGPQVDTSKAGVVASQDQVDDLLDSLGF
	21 -> 21	I	I → T: gain of function; smooth swimming; increased counterclockwise rotation of flagella. See also \|CITS: [17998207][21764922]\|
	24 -> 24	L	L → P: gain of function; smooth swimming; increased dephosphorylation of CheY-phosphate in vitro
	25 -> 25	T	T → P: gain of function; smooth swimming
	27 -> 27	M	M → V: gain of function; smooth swimming

Type	Positions	Sequence	Comment
	17 -> 214	IIARIGSLTRMLRDSLRELGLDQAIAEAAEAIPDARDRLYYVVQMTAQAAERALNSVEASQPHQDQMEKSAKALTQRWDDWFADPIDLADARELVTDTRQFLADVPAHTSFTNAQLLEIMMAQDFQDLTGQVIKRMMDVIQEIERQLLMVLLENIPEQESRPKRENQSLLNGPQVDTSKAGVVASQDQVDDLLDSLGF
	21 -> 21	I	I → T: gain of function; smooth swimming; increased counterclockwise rotation of flagella. See also \|CITS: [17998207][21764922]\|
	24 -> 24	L	L → P: gain of function; smooth swimming; increased dephosphorylation of CheY-phosphate in vitro
	25 -> 25	T	T → P: gain of function; smooth swimming
	27 -> 27	M	M → V: gain of function; smooth swimming
	28 -> 28	L	L → P: gain of function; smooth swimming; increased dephosphorylation of CheY-phosphate in vitro
	29 -> 29	R	R → C: gain of function
	37 -> 37	L	L → P: gain of function; smooth swimming
	40 -> 40	A	A → V: gain of function; smooth swimming
	50 -> 50	D	D → G: gain of function
	54 -> 54	R	R → S: gain of function; smooth swimming
	62 -> 62	T	T → A: loss of function (medium); tumbly swimming; reduced dephosphorylation of CheY-phosphate in vitro
	65 -> 65	A	loss of function mutation; defective in ability to dephosporylate CheY-phosphate; fails to oligomerize.
	90 -> 90	L	loss of function mutation; defective in ability to dephosporylate CheY-phosphate; loss of localization to the cell pole; fails to oligomerize.
	94 -> 94	W	UniProt: Loss of localization to the cell pole..
	115 -> 115	R	R → P: loss of function (strong); tumbly swimming; reduced dephosphorylation of CheY-phosphate in vitro
	117 -> 117	F	UniProt: Loss of localization to the cell pole..
	118 -> 118	L	L → P: loss of function (strong); tumbly swimming; reduced dephosphorylation of CheY-phosphate in vitro
	119 -> 119	A	UniProt: In Ref. 1; AAA23571..
	130 -> 130	A	UniProt: In Ref. 1; AAA23571..
	133 -> 133	L	L → P: loss of function (strong); tumbly swimming; reduced dephosphorylation of CheY-phosphate in vitro
	143 -> 143	D	UniProt: Loss of function. Fails to oligomerize..
	146 -> 146	G	G → R: loss of function (medium); tumbly swimming; reduced dephosphorylation of CheY-phosphate in vitro
	147 -> 147	Q	UniProt: Severely diminished function, exclusive clockwise flagellar rotation..
	149 -> 149	I	I → T: loss of function (medium); tumbly swimming; reduced dephosphorylation of CheY-phosphate in vitro
	152 -> 152	M	M → T: gain of function; smooth swimming
	155 -> 155	V	V → A: gain of function; smooth swimming
	158 -> 158	E	E → G: gain of function; smooth swimming
	166 -> 166	V	V → E: gain of function; smooth swimming; increased dephosphorylation of CheY-phosphate in vitro
	170 -> 170	N	N → D: gain of function; smooth swimming
	174 -> 199	QESRPKRENQSLLNGPQVDTSKAGVV	UniProt: Disordered; Sequence Annotation Type: region of interest.
	181 -> 199	ENQSLLNGPQVDTSKAGVV	UniProt: Polar residues; Sequence Annotation Type: compositionally biased region.
	188 -> 188	G	loss of function mutation; defective in ability to dephosporylate CheY-phosphate
	205 -> 205	V	loss of function mutation; severely impairs the interaction the interaction with CheY-P.

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:1902021 - regulation of bacterial-type flagellum-dependent cell 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:

ALPHAFOLD:

DIP:

ECOCYC:

ECOLIWIKI:

INTERPRO:

MODBASE:

PDB:

PFAM:

PRIDE:

PRODB:

REFSEQ:

SMR:

UNIPROT:

Operon

Name:

tar-tap-cheRBYZ

Operon arrangement:

Transcription unit	Promoter
tar-tap-cheRBYZ	tarp

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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