RegulonDB RegulonDB 9.4:Regulon Page

OmpR DNA-binding transcriptional dual regulator

Synonyms: OmpR-Phosphorylated, OmpR
The response regulator OmpR, for Outer membrane protein Regulator, [35, 36, 37] belongs to the two-component system EnvZ/OmpR [38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49] EnvZ is an osmosensor histidine kinase and is known to be a transmembrane protein composed of three domains: an external sensory domain (amino terminal), a cytoplasmic transmitter domain (carboxyl terminal), and a transmembrane hydrophobic central domain [50, 51, 52] The sensor domain responds to changes in extracellular osmolarity. EnvZ and OmpR comprise a signal transduction system where the signal generated by the periplasmic receptor affects through a protein-protein interaction the EnvZ cytoplasmic component, which is transmitted via autophosphorylation of histidine kinase to the response regulator OmpR [18, 38, 39, 40, 41, 42, 46, 47, 49, 53, 54, 55] OmpR is localized preferentially at the nucleoid edges and close to the cell membrane under low-salt and acidic conditions [56]
Phosphorylated OmpR controls the transcriptional expression of several genes and operons whose products are involved in adaptation to changes in osmolarity, such as major outer membrane porins [19, 40, 44, 57, 58, 59, 60, 61, 62], and it negatively regulates the expression of flagella [16] promotes biofilm formation [12] increases curli gene expression [10, 63] increases expression of several drug exporter genes [64] and confers increased beta-lactam resistance [65] among other effects [9, 17, 34, 66] When the genes csgD or ompR are overexpressed, the curli number is increased, with higher levels found in cells overexpressing the csgD gene, and there is not an additive effect on the curli number or structure in a strain overexpressing both the csgD and ompR genes.
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Transcription factor      
TF conformation(s):
Name Conformation Type TF-Effector Interaction Type Apo/Holo Conformation Evidence (Confirmed, Strong, Weak) References
OmpR Non-Functional   Apo [BPP], [GEA], [IPI] [1], [2], [3], [4], [5], [6], [7], [8]
OmpR-Phosphorylated Functional Covalent Holo [BPP], [GEA], [IPI] [1], [2], [3], [4], [5], [6], [7], [8]
Evolutionary Family: OmpR
Sensing class: External-Two-component systems
Connectivity class: Local Regulator
Gene name: ompR
  Genome position: 3535865-3536584
  Length: 720 bp / 239 aa
Operon name: ompR-envZ
TU(s) encoding the TF:
Transcription unit        Promoter

Regulated gene(s) bolA, csgD, csgE, csgF, csgG, dtpA, ecnB, fadL, flhC, flhD, micF, nmpC, ompC, ompF, omrA, omrB, pgaA, pgaB, pgaC, pgaD, sra
Multifun term(s) of regulated gene(s) MultiFun Term (List of genes associated to the multifun term)
Transcription related (4)
activator (4)
repressor (4)
Beta barrel porins (The Outer Membrane Porin (OMP) Functional Superfamily) (4)
antisense RNA (4)
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Regulated operon(s) bdm-sra, bolA, csgDEFG, dtpA, ecnAB, fadL, flhDC, micF, nmpC, ompC, ompF, omrA, omrB, pgaABCD
First gene in the operon(s) bolA, csgD, dtpA, ecnB, fadL, flhD, micF, nmpC, ompC, ompF, omrA, omrB, pgaA, sra
Simple and complex regulons AcrR,CRP,FliZ,Fur,H-NS,HdfR,IHF,LrhA,MatA,OmpR,QseB,RcsB,YjjQ
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Simple and complex regulatory phrases Regulatory phrase (List of promoters regulated by the phrase)

Transcription factor binding sites (TFBSs) arrangements       

  Functional conformation Function Promoter Sigma factor Central Rel-Pos Distance to first Gene Genes Sequence
LeftPos RightPos Evidence (Confirmed, Strong, Weak) References
  OmpR-Phosphorylated repressor bolAp1 Sigma38 -47.5 -85.5 bolA
454377 454396 [BPP], [HIBSCS] [9]
  OmpR-Phosphorylated activator csgDp1 Sigma38 -49.5 -197.5 csgD, csgE, csgF, csgG
1103384 1103403 [BPP], [GEA], [HIBSCS] [10], [11], [12]
  OmpR-Phosphorylated repressor ecnBp Sigma38 18.5 -26.5 ecnB
4376517 4376536 [HIBSCS] [13]
  OmpR-Phosphorylated repressor fadLp Sigma38 -149.5 -250.5 fadL
2461046 2461065 [HIBSCS], [SM] [14], [15]
  OmpR-Phosphorylated repressor fadLp Sigma38 -60.5 -161.5 fadL
2461135 2461154 [GEA], [HIBSCS] [15]
  OmpR-Phosphorylated repressor fadLp Sigma38 69.5 -32.5 fadL
2461264 2461283 [GEA], [HIBSCS] [15]
  OmpR-Phosphorylated repressor fadLp Sigma38 119.5 17.5 fadL
2461314 2461333 [GEA], [HIBSCS] [15]
  OmpR-Phosphorylated repressor flhDp Sigma70 -145.5 -343.5 flhD, flhC
1978531 1978550 [HIBSCS] [16]
  OmpR-Phosphorylated repressor flhDp Sigma70 18.5 -180.5 flhD, flhC
1978368 1978387 [HIBSCS] [16]
  OmpR-Phosphorylated activator micFp Sigma70 -206.5 -206.5 micF
2312868 2312887 [BPP], [GEA], [HIBSCS], [SM] [6], [17], [18], [19]
  OmpR-Phosphorylated activator micFp Sigma70 -186.5 -186.5 micF
2312888 2312907 [BPP], [GEA], [HIBSCS], [SM] [6], [7], [17], [19]
  OmpR-Phosphorylated activator micFp Sigma70 -165.5 -165.5 micF
2312909 2312928 [BPP], [GEA], [HIBSCS], [SM] [6], [7], [17], [19]
  OmpR-Phosphorylated repressor nmpCp nd -45.5 -90.5 nmpC
576906 576925 [HIBSCS], [SM] [20]
  OmpR-Phosphorylated activator ompCp1 Sigma70 -88.5 -169.5 ompC
2312909 2312928 [BPP], [GEA], [HIBSCS], [SM] [6], [7], [17], [19], [21]
  OmpR-Phosphorylated activator ompCp1 Sigma70 -67.5 -148.5 ompC
2312888 2312907 [BPP], [GEA], [HIBSCS], [SM] [6], [7], [17], [19], [21]
  OmpR-Phosphorylated activator ompCp1 Sigma70 -47.5 -128.5 ompC
2312868 2312887 [BPP], [GEA], [HIBSCS], [SM] [6], [17], [18], [19], [21]
  OmpR-Phosphorylated repressor ompFp Sigma38 -370.5 -480.5 ompF
987453 987472 [BPP], [GEA] [19], [21], [22], [23], [24]
  OmpR-Phosphorylated activator ompFp Sigma38 -90.5 -200.5 ompF
987173 987192 [BPP], [GEA], [HIBSCS], [SM] [6], [7], [18], [19], [25], [26], [27], [28]
  OmpR-Phosphorylated dual ompFp Sigma38 -70.5 -180.5 ompF
987153 987172 [BCE], [BPP], [GEA], [HIBSCS], [SM] [6], [7], [18], [19], [21], [25], [26], [27], [28], [29], [30]
  OmpR-Phosphorylated dual ompFp Sigma38 -50.5 -160.5 ompF
987133 987152 [AIBSCS], [BPP], [GEA], [SM] [6], [7], [18], [19], [22], [23], [24], [25], [26], [27], [28], [29]
  OmpR-Phosphorylated activator omrAp nd -70.5 -70.5 omrA
2976250 2976269 [GEA], [HIBSCS] [31]
  OmpR-Phosphorylated activator omrBp nd -71.5 -71.5 omrB
2976447 2976466 [GEA], [HIBSCS] [31]
  OmpR-Phosphorylated repressor pgaAp nd -31.5 -265.5 pgaA, pgaB, pgaC, pgaD
1092545 1092564 [BPP], [GEA], [HIBSCS] [32]
  OmpR-Phosphorylated repressor srap Sigma38 nd nd sra nd nd [GEA] [33]
  OmpR-Phosphorylated activator tppBp Sigma70 -45.5 -143.5 dtpA
1712616 1712635 [BPP], [GEA] [34]

Alignment and PSSM for OmpR TFBSs    

Aligned TFBS of OmpR   

Position weight matrix (PWM).   
A	9	14	6	10	1	0	6	15	16	3	6	16	14	13	8	6	3	8	11
C	0	2	5	4	4	0	3	0	1	15	8	0	3	0	1	4	0	1	0
G	2	2	1	4	1	17	0	0	0	0	2	2	2	5	2	5	0	3	0
T	9	2	8	2	14	3	11	5	3	2	4	2	1	2	9	5	17	8	9

PWM logo   


Evolutionary conservation of regulatory elements    
     Note: Evolutionary conservation of regulatory interactions and promoters is limited to gammaproteobacteria.
TF-target gene evolutionary conservation
Promoter-target gene evolutionary conservation


 [BPP] Binding of purified proteins

 [GEA] Gene expression analysis

 [IPI] Inferred from physical interaction

 [HIBSCS] Human inference based on similarity to consensus sequences

 [SM] Site mutation

 [BCE] Binding of cellular extracts

 [AIBSCS] Automated inference based on similarity to consensus sequences


 [1] Aiba H., Nakasai F., Mizushima S., Mizuno T., 1989, Evidence for the physiological importance of the phosphotransfer between the two regulatory components, EnvZ and OmpR, in osmoregulation in Escherichia coli., J Biol Chem. 264(24):14090-4

 [2] Forst S, Delgado J, Rampersaud A, Inouye M., 1990, In vivo phosphorylation of OmpR, the transcription activator of the ompF and ompC genes in Escherichia coli., J Bacteriol.

 [3] Huang KJ, Lan CY, Igo MM., 1997, Phosphorylation stimulates the cooperative DNA-binding properties of the transcription factor OmpR., Proc Natl Acad Sci U S A.

 [4] Kenney LJ., Bauer MD., Silhavy TJ., 1995, Phosphorylation-dependent conformational changes in OmpR, an osmoregulatory DNA-binding protein of Escherichia coli., Proc Natl Acad Sci U S A. 92(19):8866-70

 [5] Martinez-Hackert E., Stock AM., 1997, The DNA-binding domain of OmpR: crystal structures of a winged helix transcription factor., Structure. 5(1):109-24

 [6] Mattison K., Oropeza R., Byers N., Kenney LJ., 2002, A phosphorylation site mutant of OmpR reveals different binding conformations at ompF and ompC., J Mol Biol. 315(4):497-511

 [7] Tsung K., Brissette RE., Inouye M., 1989, Identification of the DNA-binding domain of the OmpR protein required for transcriptional activation of the ompF and ompC genes of Escherichia coli by in vivo DNA footprinting., J Biol Chem. 264(17):10104-9

 [8] Yamamoto K., Hirao K., Oshima T., Aiba H., Utsumi R., Ishihama A., 2005, Functional characterization in vitro of all two-component signal transduction systems from Escherichia coli., J Biol Chem. 280(2):1448-56

 [9] Yamamoto K., Nagura R., Tanabe H., Fujita N., Ishihama A., Utsumi R., 2000, Negative regulation of the bolA1p of Escherichia coli K-12 by the transcription factor OmpR for osmolarity response genes., FEMS Microbiol Lett. 186(2):257-62

 [10] Jubelin G., Vianney A., Beloin C., Ghigo JM., Lazzaroni JC., Lejeune P., Dorel C., 2005, CpxR/OmpR interplay regulates curli gene expression in response to osmolarity in Escherichia coli., J Bacteriol. 187(6):2038-49

 [11] Ogasawara H., Yamada K., Kori A., Yamamoto K., Ishihama A., 2010, Regulation of the Escherichia coli csgD promoter: interplay between five transcription factors., Microbiology. 156(Pt 8):2470-83

 [12] Prigent-Combaret C., Brombacher E., Vidal O., Ambert A., Lejeune P., Landini P., Dorel C., 2001, Complex regulatory network controls initial adhesion and biofilm formation in Escherichia coli via regulation of the csgD gene., J Bacteriol. 183(24):7213-23

 [13] Bishop RE., Leskiw BK., Hodges RS., Kay CM., Weiner JH., 1998, The entericidin locus of Escherichia coli and its implications for programmed bacterial cell death., J Mol Biol. 280(4):583-96

 [14] Black PN., 1991, Primary sequence of the Escherichia coli fadL gene encoding an outer membrane protein required for long-chain fatty acid transport., J Bacteriol. 173(2):435-42

 [15] Higashitani A., Nishimura Y., Hara H., Aiba H., Mizuno T., Horiuchi K., 1993, Osmoregulation of the fatty acid receptor gene fadL in Escherichia coli., Mol Gen Genet. 240(3):339-47

 [16] Shin S., Park C., 1995, Modulation of flagellar expression in Escherichia coli by acetyl phosphate and the osmoregulator OmpR., J Bacteriol. 177(16):4696-702

 [17] Coyer J., Andersen J., Forst SA., Inouye M., Delihas N., 1990, micF RNA in ompB mutants of Escherichia coli: different pathways regulate micF RNA levels in response to osmolarity and temperature change., J Bacteriol. 172(8):4143-50

 [18] 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

 [19] Yoshida T., Qin L., Egger LA., Inouye M., 2006, Transcription regulation of ompF and ompC by a single transcription factor, OmpR., J Biol Chem. 281(25):17114-23

 [20] Coll JL., Heyde M., Portalier R., 1994, Expression of the nmpC gene of Escherichia coli K-12 is modulated by external pH. Identification of cis-acting regulatory sequences involved in this regulation., Mol Microbiol. 12(1):83-93

 [21] Oshima T., Aiba H., Masuda Y., Kanaya S., Sugiura M., Wanner BL., Mori H., Mizuno T., 2002, Transcriptome analysis of all two-component regulatory system mutants of Escherichia coli K-12., Mol Microbiol. 46(1):281-91

 [22] Huang KJ., Schieberl JL., Igo MM., 1994, A distant upstream site involved in the negative regulation of the Escherichia coli ompF gene., J Bacteriol. 176(5):1309-15

 [23] Rampersaud A., Harlocker SL., Inouye M., 1994, The OmpR protein of Escherichia coli binds to sites in the ompF promoter region in a hierarchical manner determined by its degree of phosphorylation., J Biol Chem. 269(17):12559-66

 [24] Slauch JM., Silhavy TJ., 1991, cis-acting ompF mutations that result in OmpR-dependent constitutive expression., J Bacteriol. 173(13):4039-48

 [25] Forst SA., Delgado J., Inouye M., 1989, DNA-binding properties of the transcription activator (OmpR) for the upstream sequences of ompF in Escherichia coli are altered by envZ mutations and medium osmolarity., J Bacteriol. 171(6):2949-55

 [26] Lan CY., Igo MM., 1998, Differential expression of the OmpF and OmpC porin proteins in Escherichia coli K-12 depends upon the level of active OmpR., J Bacteriol. 180(1):171-4

 [27] Rampersaud A., Norioka S., Inouye M., 1989, Characterization of OmpR binding sequences in the upstream region of the ompF promoter essential for transcriptional activation., J Biol Chem. 264(31):18693-700

 [28] Sato M., Machida K., Arikado E., Saito H., Kakegawa T., Kobayashi H., 2000, Expression of outer membrane proteins in Escherichia coli growing at acid pH., Appl Environ Microbiol. 66(3):943-7

 [29] Forst S., Kalve I., Durski W., 1995, Molecular analysis of OmpR binding sequences involved in the regulation of ompF in Escherichia coli., FEMS Microbiol Lett. 131(2):147-51

 [30] Ramani N., Huang L., Freundlich M., 1992, In vitro interactions of integration host factor with the ompF promoter-regulatory region of Escherichia coli., Mol Gen Genet. 231(2):248-55

 [31] Guillier M., Gottesman S., 2006, Remodelling of the Escherichia coli outer membrane by two small regulatory RNAs., Mol Microbiol. 59(1):231-47

 [32] Oropeza R., Salgado-Bravo R., Calva E., 2015, Deletion analysis of RcsC reveals a novel signalling pathway controlling poly-N-acetylglucosamine synthesis and biofilm formation in Escherichia coli., Microbiology. 161(Pt 4):903-13

 [33] Izutsu K., Wada C., Komine Y., Sako T., Ueguchi C., Nakura S., Wada A., 2001, Escherichia coli ribosome-associated protein SRA, whose copy number increases during stationary phase., J Bacteriol. 183(9):2765-73

 [34] Goh EB., Siino DF., Igo MM., 2004, The Escherichia coli tppB (ydgR) gene represents a new class of OmpR-regulated genes., J Bacteriol. 186(12):4019-24

 [35] Taylor RK., Hall MN., Enquist L., Silhavy TJ., 1981, Identification of OmpR: a positive regulatory protein controlling expression of the major outer membrane matrix porin proteins of Escherichia coli K-12., J Bacteriol. 147(1):255-8

 [36] Mizuno T., Wurtzel ET., Inouye M., 1982, Cloning of the regulatory genes (ompR and envZ) for the matrix proteins of the Escherichia coli outer membrane., J Bacteriol. 150(3):1462-6

 [37] Kojetin DJ., Sullivan DM., Thompson RJ., Cavanagh J., 2007, Classification of response regulators based on their surface properties., Methods Enzymol. 422:141-69

 [38] 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

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

 [40] Kanamaru K., Mizuno T., 1992, Signal transduction and osmoregulation in Escherichia coli: a novel mutant of the positive regulator, OmpR, that functions in a phosphorylation-independent manner., J Biochem. 111(4):425-30

 [41] Forst SA., Roberts DL., 1994, Signal transduction by the EnvZ-OmpR phosphotransfer system in bacteria., Res Microbiol. 145(5-6):363-73

 [42] Matsubara M., Mizuno T., 1999, EnvZ-independent phosphotransfer signaling pathway of the OmpR-mediated osmoregulatory expression of OmpC and OmpF in Escherichia coli., Biosci Biotechnol Biochem. 63(2):408-14

 [43] Matsubara M., Kitaoka SI., Takeda SI., Mizuno T., 2000, Tuning of the porin expression under anaerobic growth conditions by his-to-Asp cross-phosphorelay through both the EnvZ-osmosensor and ArcB-anaerosensor in Escherichia coli., Genes Cells. 5(7):555-69

 [44] Cai SJ., Inouye M., 2002, EnvZ-OmpR interaction and osmoregulation in Escherichia coli., J Biol Chem. 277(27):24155-61

 [45] Mattison K., Oropeza R., Kenney LJ., 2002, The linker region plays an important role in the interdomain communication of the response regulator OmpR., J Biol Chem. 277(36):32714-21

 [46] Yoshida T., Qin L., Inouye M., 2002, Formation of the stoichiometric complex of EnvZ, a histidine kinase, with its response regulator, OmpR., Mol Microbiol. 46(5):1273-82

 [47] Maris AE., Walthers D., Mattison K., Byers N., Kenney LJ., 2005, The response regulator OmpR oligomerizes via beta-sheets to form head-to-head dimers., J Mol Biol. 350(5):843-56

 [48] Batchelor E., Goulian M., 2006, Imaging OmpR localization in Escherichia coli., Mol Microbiol. 59(6):1767-78

 [49] Yoshida T., Cai S., Inouye M., 2002, Interaction of EnvZ, a sensory histidine kinase, with phosphorylated OmpR, the cognate response regulator., Mol Microbiol. 46(5):1283-94

 [50] 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

 [51] Egger LA., Inouye M., 1997, Purification and characterization of the periplasmic domain of EnvZ osmosensor in Escherichia coli., Biochem Biophys Res Commun. 231(1):68-72

 [52] Khorchid A., Inouye M., Ikura M., 2005, Structural characterization of Escherichia coli sensor histidine kinase EnvZ: the periplasmic C-terminal core domain is critical for homodimerization., Biochem J. 385(Pt 1):255-64

 [53] Nakashima K., Kanamaru K., Aiba H., Mizuno T., 1991, Osmoregulatory expression of the porin genes in Escherichia coli: evidence for signal titration in the signal transduction through EnvZ-OmpR phosphotransfer., FEMS Microbiol Lett. 66(1):43-7

 [54] Qin L., Dutta R., Kurokawa H., Ikura M., Inouye M., 2000, A monomeric histidine kinase derived from EnvZ, an Escherichia coli osmosensor., Mol Microbiol. 36(1):24-32

 [55] Kenney LJ., 2002, Structure/function relationships in OmpR and other winged-helix transcription factors., Curr Opin Microbiol. 5(2):135-41

 [56] Foo YH., Spahn C., Zhang H., Heilemann M., Kenney LJ., 2015, Single cell super-resolution imaging of E. coli OmpR during environmental stress., Integr Biol (Camb)

 [57] Garrett S., Taylor RK., Silhavy TJ., Berman ML., 1985, Isolation and characterization of delta ompB strains of Escherichia coli by a general method based on gene fusions., J Bacteriol. 162(2):840-4

 [58] Nara F., Matsuyama S., Mizuno T., Mizushima S., 1986, Molecular analysis of mutant ompR genes exhibiting different phenotypes as to osmoregulation of the ompF and ompC genes of Escherichia coli., Mol Gen Genet. 202(2):194-9

 [59] 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 (Tokyo). 101(2):387-96

 [60] Csonka LN., Hanson AD., 1991, Prokaryotic osmoregulation: genetics and physiology., Annu Rev Microbiol. 45:569-606

 [61] Maeda S., Takayanagi K., Nishimura Y., Maruyama T., Sato K., Mizuno T., 1991, Activation of the osmoregulated ompC gene by the OmpR protein in Escherichia coli: a study involving synthetic OmpR-binding sequences., J Biochem. 110(3):324-7

 [62] Huang KJ., Igo MM., 1996, Identification of the bases in the ompF regulatory region, which interact with the transcription factor OmpR., J Mol Biol. 262(5):615-28

 [63] Vidal O., Longin R., Prigent-Combaret C., Dorel C., Hooreman M., Lejeune P., 1998, Isolation of an Escherichia coli K-12 mutant strain able to form biofilms on inert surfaces: involvement of a new ompR allele that increases curli expression., J Bacteriol. 180(9):2442-9

 [64] Hirakawa H., Nishino K., Hirata T., Yamaguchi A., 2003, Comprehensive studies of drug resistance mediated by overexpression of response regulators of two-component signal transduction systems in Escherichia coli., J Bacteriol. 185(6):1851-6

 [65] Hirakawa H., Nishino K., Yamada J., Hirata T., Yamaguchi A., 2003, Beta-lactam resistance modulated by the overexpression of response regulators of two-component signal transduction systems in Escherichia coli., J Antimicrob Chemother. 52(4):576-82

 [66] Guillier M., Gottesman S., 2008, The 5' end of two redundant sRNAs is involved in the regulation of multiple targets, including their own regulator., Nucleic Acids Res. 36(21):6781-94

 [67] Perni S., Preedy EC., Landini P., Prokopovich P., 2016, Influence of csgD and ompR on Nanomechanics, Adhesion Forces, and Curli Properties of E. coli., Langmuir. 32(31):7965-74

 [68] Brissette RE., Tsung K., Inouye M., 1992, Mutations in a central highly conserved non-DNA-binding region of OmpR, an Escherichia coli transcriptional activator, influence its DNA-binding ability., J Bacteriol. 174(15):4907-12

 [69] Kato N., Tsuzuki M., Aiba H., Mizuno T., 1995, Gene activation by the Escherichia coli positive regulator OmpR: a mutational study of the DNA-binding domain of OmpR., Mol Gen Genet. 248(4):399-406

 [70] Kondo H., Nakagawa A., Nishihira J., Nishimura Y., Mizuno T., Tanaka I., 1997, Escherichia coli positive regulator OmpR has a large loop structure at the putative RNA polymerase interaction site., Nat Struct Biol. 4(1):28-31

 [71] Head CG., Tardy A., Kenney LJ., 1998, Relative binding affinities of OmpR and OmpR-phosphate at the ompF and ompC regulatory sites., J Mol Biol. 281(5):857-70

 [72] Rhee JE., Sheng W., Morgan LK., Nolet R., Liao X., Kenney LJ., 2008, Amino acids important for DNA recognition by the response regulator OmpR., J Biol Chem. 283(13):8664-77

 [73] Harrison-McMonagle P., Denissova N., Martinez-Hackert E., Ebright RH., Stock AM., 1999, Orientation of OmpR monomers within an OmpR:DNA complex determined by DNA affinity cleaving., J Mol Biol. 285(2):555-66

 [74] Harlocker SL., Bergstrom L., Inouye M., 1995, Tandem binding of six OmpR proteins to the ompF upstream regulatory sequence of Escherichia coli., J Biol Chem. 270(45):26849-56

 [75] Barbieri CM., Wu T., Stock AM., 2013, Comprehensive analysis of OmpR phosphorylation, dimerization, and DNA binding supports a canonical model for activation., J Mol Biol. 425(10):1612-26

 [76] Siryaporn A., Goulian M., 2008, Cross-talk suppression between the CpxA-CpxR and EnvZ-OmpR two-component systems in E. coli., Mol Microbiol. 70(2):494-506

 [77] Quinn HJ., Cameron AD., Dorman CJ., 2014, Bacterial regulon evolution: distinct responses and roles for the identical OmpR proteins of Salmonella Typhimurium and Escherichia coli in the acid stress response., PLoS Genet. 10(3):e1004215