RegulonDB RegulonDB 10.9: Gene Form
   

envZ gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

pck envZ ompR greB IHF CRP IHF IHF OmrB OmrA TSS_4004 TSS_4004 yhgFp2 yhgFp2 greBp7 greBp7 ompRp4 ompRp4 greBp8 greBp8 ompRp1 ompRp1 ompRp2 ompRp2 ompRp3 ompRp3 TSS_4002 TSS_4002 TSS_4001 TSS_4001

Gene      
Name: envZ    Texpresso search in the literature
Synonym(s): ECK3391, EG10269, b3404, ompB, perA, tpo
Genome position(nucleotides): 3534516 <-- 3535868 Genome Browser
Strand: reverse
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
57.06
External database links:  
ASAP:
ABE-0011108
CGSC:
807
ECHOBASE:
EB0265
ECOLIHUB:
envZ
OU-MICROARRAY:
b3404
STRING:
511145.b3404
COLOMBOS: envZ


Product      
Name: sensor histidine kinase EnvZ
Synonym(s): EnvZ, OmpB, PerA, Tpo
Sequence: Get amino acid sequence Fasta Format
Cellular location: periplasmic space,cytosol,inner membrane
Molecular weight: 50.334
Isoelectric point: 6.81
Motif(s):
 
Type Positions Sequence
16 -> 35 LLLIVTLLFASLVTTYLVVL
180 -> 232 RIQNRPLVDLEHAALQVGKGIIPPPLREYGASEVRSVTRAFNHMAAGVKQLAD
242 -> 242 S
336 -> 438 SIKRAVANMVVNAARYGNGWIKVSSGTEPNRAWFQVEDDGPGIAPEQRKHLFQPFVRGDSARTISGTGLGLAIVQRIVDNHNGMLELGTSERGGLSIRAWLPV
351 -> 351 Y

 

Classification:
Multifun Terms (GenProtEC)  
  2 - information transfer --> 2.3 - protein related --> 2.3.3 - posttranslational modification
  3 - regulation --> 3.1 - type of regulation --> 3.1.2 - transcriptional level --> 3.1.2.4 - complex regulation --> 3.1.2.4.3 - two component regulatory systems (external signal)
  3 - regulation --> 3.1 - type of regulation --> 3.1.3 - posttranscriptional --> 3.1.3.2 - covalent modification, demodification, maturation
  6 - cell structure --> 6.1 - membrane
Gene Ontology Terms (GO)  
cellular_component GO:0005829 - cytosol
GO:0016020 - membrane
GO:0030288 - outer membrane-bounded periplasmic space
GO:0005886 - plasma membrane
GO:0005887 - integral component of plasma membrane
GO:0016021 - integral component of membrane
molecular_function GO:0005515 - protein binding
GO:0016740 - transferase activity
GO:0016772 - transferase activity, transferring phosphorus-containing groups
GO:0016301 - kinase activity
GO:0004721 - phosphoprotein phosphatase activity
GO:0000166 - nucleotide binding
GO:0005524 - ATP binding
GO:0000155 - phosphorelay sensor kinase activity
GO:0004673 - protein histidine kinase activity
GO:0042802 - identical protein binding
GO:0042803 - protein homodimerization activity
biological_process GO:0006970 - response to osmotic stress
GO:0006470 - protein dephosphorylation
GO:0016310 - phosphorylation
GO:0047484 - regulation of response to osmotic stress
GO:0000160 - phosphorelay signal transduction system
GO:0007165 - signal transduction
GO:0046777 - protein autophosphorylation
GO:0018106 - peptidyl-histidine phosphorylation
GO:0023014 - signal transduction by protein phosphorylation
Note(s): Note(s): ...[more].
Reference(s): [1] Aiba H., et al., 1990
[2] Baumgartner JW., et al., 1994
[3] Botelho SC., et al., 2015
[4] Comeau DE., et al., 1988
[5] Darcan C., et al., 2009
[6] Dutta R., et al., 1996
[7] Foo YH., et al., 2015
[8] Forst S., et al., 1989
[9] Hall MN., et al., 1979
[10] Harlocker SL., et al., 1993
[11] Heininger A., et al., 2016
[12] Hwang E., et al., 2017
[13] Igo MM., et al., 1988
[14] Kim SK., et al., 1996
[15] King ST., et al., 2007
[16] Kishii R., et al., 2007
[17] Matsuyama S., et al., 1986
[18] Mattison K., et al., 2002
[19] Mizuno T., et al., 1990
[20] Mizuno T., et al., 1987
[21] Olshefsky A., et al., 2016
[22] Qin L., et al., 2003
[23] Qin L., et al., 2001
[24] Rampersaud A., et al., 1991
[25] Sarma V., et al., 1977
[26] Slauch JM., et al., 1988
[27] Slauch JM., et al., 1989
[28] Tokishita S., et al., 1991
[29] Tokishita S., et al., 1994
[30] Tokishita S., et al., 1990
[31] Tomomori C., et al., 1999
[32] Wang LC., et al., 2015
[33] Waukau J., et al., 1992
[34] Yaku H., et al., 1997
[35] Yoshida T., et al., 2007
[36] Yoshida T., et al., 2007
[37] Zhu Y., et al., 2002
External database links:  
DIP:
DIP-48357N
ECOCYC:
ENVZ-MONOMER
ECOLIWIKI:
b3404
INTERPRO:
IPR003660
INTERPRO:
IPR036097
INTERPRO:
IPR036890
INTERPRO:
IPR003661
INTERPRO:
IPR004358
INTERPRO:
IPR005467
INTERPRO:
IPR003594
MINT:
P0AEJ4
MODBASE:
P0AEJ4
PDB:
5XGA
PDB:
5B1O
PDB:
5B1N
PDB:
4KP4
PDB:
4CTI
PDB:
3ZRX
PDB:
3ZRW
PDB:
3ZRV
PDB:
3ZCC
PDB:
1NJV
PDB:
1JOY
PDB:
1BXD
PFAM:
PF02518
PFAM:
PF00672
PFAM:
PF00512
PRIDE:
P0AEJ4
PRINTS:
PR00344
PRODB:
PRO_000022527
PROSITE:
PS50885
PROSITE:
PS50109
REFSEQ:
NP_417863
SMART:
SM00304
SMART:
SM00388
SMART:
SM00387
SMR:
P0AEJ4
SWISSMODEL:
P0AEJ4
UNIPROT:
P0AEJ4


Operon      
Name: ompR-envZ         
Operon arrangement:
Transcription unit        Promoter
ompR-envZ
ompR-envZ
ompR-envZ
ompR-envZ


Transcriptional Regulation      
Display Regulation             
Activated by: CRP
Repressed by: CRP, IHF


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
  promoter TSS_4001 3536371 reverse nd [RS-EPT-CBR] [38]
  promoter TSS_4002 3536377 reverse nd [RS-EPT-CBR] [38]
  promoter greBp8 3536744 forward Similarity to the consensus
Read more >
[ICWHO] [39]
  promoter greBp7 3536780 forward Similarity to the consensus
Read more >
[ICWHO] [39]
  promoter yhgFp2 3537176 forward Similarity to the consensus
Read more >
[ICWHO] [39]
  promoter TSS_4004 3537268 forward nd [RS-EPT-CBR] [38]


Evidence    

 [RS-EPT-CBR] RNA-seq using two enrichment strategies for primary transcripts and consistent biological replicates

 [ICWHO] Inferred computationally without human oversight



Reference(s)    

 [1] Aiba H., Mizuno T., 1990, Phosphorylation of a bacterial activator protein, OmpR, by a protein kinase, EnvZ, stimulates the transcription of the ompF and ompC genes in Escherichia coli., FEBS Lett 261(1):19-22

 [2] Baumgartner JW., Kim C., Brissette RE., Inouye M., Park C., Hazelbauer GL., 1994, Transmembrane signalling by a hybrid protein: communication from the domain of chemoreceptor Trg that recognizes sugar-binding proteins to the kinase/phosphatase domain of osmosensor EnvZ., J Bacteriol 176(4):1157-63

 [3] Botelho SC., Enquist K., von Heijne G., Draheim RR., 2015, Differential repositioning of the second transmembrane helices from E. coli Tar and EnvZ upon moving the flanking aromatic residues., Biochim Biophys Acta 1848(2):615-21

 [4] Comeau DE., Inouye M., 1988, A novel method for the cloning of chromosomal mutations in a single step: isolation of two mutant alleles of envZ, an osmoregulatory gene from Escherichia coli., Mol Gen Genet 213(1):166-9

 [5] Darcan C., Ozkanca R., Idil O., Flint KP., 2009, Viable but non-culturable state (VBNC) of Escherichia coli related to EnvZ under the effect of pH, starvation and osmotic stress in sea water., Pol J Microbiol 58(4):307-17

 [6] Dutta R., Inouye M., 1996, Reverse phosphotransfer from OmpR to EnvZ in a kinase-/phosphatase+ mutant of EnvZ (EnvZ.N347D), a bifunctional signal transducer of Escherichia coli., J Biol Chem 271(3):1424-9

 [7] Foo YH., Gao Y., Zhang H., Kenney LJ., 2015, Cytoplasmic sensing by the inner membrane histidine kinase EnvZ., Prog Biophys Mol Biol 118(3):119-29

 [8] Forst S., Delgado J., Inouye M., 1989, Phosphorylation of OmpR by the osmosensor EnvZ modulates expression of the ompF and ompC genes in Escherichia coli., Proc Natl Acad Sci U S A 86(16):6052-6

 [9] Hall MN., Silhavy TJ., 1979, Transcriptional regulation of Escherichia coli K-12 major outer membrane protein 1b., J Bacteriol 140(2):342-50

 [10] Harlocker SL., Rampersaud A., Yang WP., Inouye M., 1993, Phenotypic revertant mutations of a new OmpR2 mutant (V203Q) of Escherichia coli lie in the envZ gene, which encodes the OmpR kinase., J Bacteriol 175(7):1956-60

 [11] Heininger A., Yusuf R., Lawrence RJ., Draheim RR., 2016, Identification of transmembrane helix 1 (TM1) surfaces important for EnvZ dimerisation and signal output., Biochim Biophys Acta 1858(8):1868-75

 [12] Hwang E., Cheong HK., Kim SY., Kwon O., Blain KY., Choe S., Yeo KJ., Jung YW., Jeon YH., Cheong C., 2017, Crystal structure of the EnvZ periplasmic domain with CHAPS., FEBS Lett 591(10):1419-1428

 [13] Igo MM., Silhavy TJ., 1988, EnvZ, a transmembrane environmental sensor of Escherichia coli K-12, is phosphorylated in vitro., J Bacteriol 170(12):5971-3

 [14] Kim SK., Wilmes-Riesenberg MR., Wanner BL., 1996, Involvement of the sensor kinase EnvZ in the in vivo activation of the response-regulator PhoB by acetyl phosphate., Mol Microbiol 22(1):135-47

 [15] King ST., Kenney LJ., 2007, Application of fluorescence resonance energy transfer to examine EnvZ/OmpR interactions., Methods Enzymol 422:352-60

 [16] Kishii R., Falzon L., Yoshida T., Kobayashi H., Inouye M., 2007, Structural and functional studies of the HAMP domain of EnvZ, an osmosensing transmembrane histidine kinase in Escherichia coli., J Biol Chem 282(36):26401-8

 [17] Matsuyama S., Mizuno T., Mizushima S., 1986, Interaction between two regulatory proteins in osmoregulatory expression of ompF and ompC genes in Escherichia coli: a novel ompR mutation suppresses pleiotropic defects caused by an envZ mutation., J Bacteriol 168(3):1309-14

 [18] Mattison K., Kenney LJ., 2002, Phosphorylation alters the interaction of the response regulator OmpR with its sensor kinase EnvZ., J Biol Chem 277(13):11143-8

 [19] Mizuno T., Mizushima S., 1990, Signal transduction and gene regulation through the phosphorylation of two regulatory components: the molecular basis for the osmotic regulation of the porin genes., Mol Microbiol 4(7):1077-82

 [20] Mizuno T., Mizushima S., 1987, Isolation and characterization of deletion mutants of ompR and envZ, regulatory genes for expression of the outer membrane proteins OmpC and OmpF in Escherichia coli., J Biochem 101(2):387-96

 [21] Olshefsky A., Shehata L., Kuldell N., 2016, Site-Directed Mutagenesis to Improve Sensitivity of a Synthetic Two-Component Signaling System., PLoS One 11(1):e0147494

 [22] Qin L., Cai S., Zhu Y., Inouye M., 2003, Cysteine-scanning analysis of the dimerization domain of EnvZ, an osmosensing histidine kinase., J Bacteriol 185(11):3429-35

 [23] Qin L., Yoshida T., Inouye M., 2001, The critical role of DNA in the equilibrium between OmpR and phosphorylated OmpR mediated by EnvZ in Escherichia coli., Proc Natl Acad Sci U S A 98(3):908-13

 [24] Rampersaud A., Inouye M., 1991, Procaine, a local anesthetic, signals through the EnvZ receptor to change the DNA binding affinity of the transcriptional activator protein OmpR., J Bacteriol 173(21):6882-8

 [25] Sarma V., Reeves P., 1977, Genetic locus (ompB) affecting a major outer-membrane protein in Escherichia coli K-12., J Bacteriol 132(1):23-7

 [26] Slauch JM., Garrett S., Jackson DE., Silhavy TJ., 1988, EnvZ functions through OmpR to control porin gene expression in Escherichia coli K-12., J Bacteriol 170(1):439-41

 [27] Slauch JM., Silhavy TJ., 1989, Genetic analysis of the switch that controls porin gene expression in Escherichia coli K-12., J Mol Biol 210(2):281-92

 [28] Tokishita S., Kojima A., Aiba H., Mizuno T., 1991, Transmembrane signal transduction and osmoregulation in Escherichia coli. Functional importance of the periplasmic domain of the membrane-located protein kinase, EnvZ., J Biol Chem 266(11):6780-5

 [29] Tokishita S., Mizuno T., 1994, Transmembrane signal transduction by the Escherichia coli osmotic sensor, EnvZ: intermolecular complementation of transmembrane signalling., Mol Microbiol 13(3):435-44

 [30] Tokishita S., Yamada H., Aiba H., Mizuno T., 1990, Transmembrane signal transduction and osmoregulation in Escherichia coli: II. The osmotic sensor, EnvZ, located in the isolated cytoplasmic membrane displays its phosphorylation and dephosphorylation abilities as to the activator protein, OmpR., J Biochem 108(3):488-93

 [31] Tomomori C., Tanaka T., Dutta R., Park H., Saha SK., Zhu Y., Ishima R., Liu D., Tong KI., Kurokawa H., Qian H., Inouye M., Ikura M., 1999, Solution structure of the homodimeric core domain of Escherichia coli histidine kinase EnvZ., Nat Struct Biol 6(8):729-34

 [32] Wang LC., Morgan LK., Godakumbura P., Kenney LJ., Anand GS., 2015, The inner membrane histidine kinase EnvZ senses osmolality via helix-coil transitions in the cytoplasm., EMBO J 34(19):2481

 [33] Waukau J., Forst S., 1992, Molecular analysis of the signaling pathway between EnvZ and OmpR in Escherichia coli., J Bacteriol 174(5):1522-7

 [34] Yaku H., Mizuno T., 1997, The membrane-located osmosensory kinase, EnvZ, that contains a leucine zipper-like motif functions as a dimer in Escherichia coli., FEBS Lett 417(3):409-13

 [35] Yoshida T., Phadtare S., Inouye M., 2007, The design and development of Tar-EnvZ chimeric receptors., Methods Enzymol 423:166-83

 [36] Yoshida T., Phadtare S., Inouye M., 2007, Functional and structural characterization of EnvZ, an osmosensing histidine kinase of E. coli., Methods Enzymol 423:184-202

 [37] Zhu Y., Inouye M., 2002, The role of the G2 box, a conserved motif in the histidine kinase superfamily, in modulating the function of EnvZ., Mol Microbiol 45(3):653-63

 [38] Salgado H, Peralta-Gil M, Gama-Castro S, Santos-Zavaleta A, Muñiz-Rascado L, García-Sotelo JS, Weiss V, Solano-Lira H, Martínez-Flores I, Medina-Rivera A, Salgado-Osorio G, Alquicira-Hernández S, Alquicira-Hernández K, López-Fuentes A, Porrón-Sotelo L, Huerta AM, Bonavides-Martínez C, Balderas-Martínez YI, Pannier L, Olvera M, Labastida A, Jiménez-Jacinto V, Vega-Alvarado L, Del Moral-Chávez V, Hernández-Alvarez A, Morett E, Collado-Vides J., 2012, RegulonDB v8.0: omics data sets, evolutionary conservation, regulatory phrases, cross-validated gold standards and more., Nucleic Acids Res.

 [39] Huerta AM., Collado-Vides J., 2003, Sigma70 promoters in Escherichia coli: specific transcription in dense regions of overlapping promoter-like signals., J Mol Biol 333(2):261-78


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