Transcription Factor

Accessions: ECK120004795 (RegulonDB 7.5)
Names: FNR
Organisms: ECK12
Libraries: RegulonDB 7.5 1
1 Salgado H, Peralta-Gil M, Gama-Castro S, Santos-Zavaleta A, Muniz-Rascado L, Garcia-Sotelo JS, Weiss V, Solano-Lira H, Martinez-Flores I, Medina-Rivera A, Salgado-Osorio G, Alquicira-Hernandez S, Alquicira-Hernandez K, Lopez-Fuentes A, Porron-Sotelo L, Huerta AM, Bonavides-Martinez C, Balderas-Martinez YI, Pannier L, Olvera M, Labastida A, Jimenez-Jacinto V, Vega-Alvarado L, Del Moral-Chavez V, Hernandez-Alvarez A, Morett E, Collado-Vides J. RegulonDB v8.0: omics data sets, evolutionary conservation, regulatory phrases, cross-validated gold standards and more. Nucleic Acids Res. 2013 Jan 1;41(D1):D203-D213. [Pubmed]
Notes: Transcription related; repressor; activator; global; anaerobic respiration; cytoplasm; response to nitric oxide; 4 iron, 4 sulfur cluster binding; iron-sulfur cluster binding; metal ion binding; regulation of transcription, DNA-dependent; intracellular; sequence-specific DNA binding transcription factor activity; DNA binding; transcription, DNA-dependent
Length: 251
Pfam Domains: 52-137 Cyclic nucleotide-binding domain
168-242 Crp-like helix-turn-helix domain
193-224 Bacterial regulatory proteins, crp family
Sequence:
(in bold interface residues)
1 MIPEKRIIRRIQSGGCAIHCQDCSISQLCIPFTLNEHELDQLDNIIERKKPIQKGQTLFK 60
61 AGDELKSLYAIRSGTIKSYTITEQGDEQITGFHLAGDLVGFDAIGSGHHPSFAQALETSM 120
121 VCEIPFETLDDLSGKMPNLRQQMMRLMSGEIKGDQDMILLLSKKNAEERLAAFIYNLSRR 180
181 FAQRGFSPREFRLTMTRGDIGNYLGLTVETISRLLGRFQKSGMLAVKGKYITIENNDALA 240
241 QLAGHTRNVA*
Interface Residues: 198, 207, 208, 209, 210, 212, 213
3D-footprint Homologues: 3iyd_H, 4i2o_B, 3e6c_C, 5i2d_R, 7pza_B, 3mzh_A
Binding Motifs: FNR tTGaTywayATCAA
Binding Sites: ECK120011231
ECK120011246
ECK120011248
ECK120011366
ECK120011368
ECK120011370
ECK120011600
ECK120011609
ECK120011878
ECK120011886
ECK120012050
ECK120012052
ECK120012056
ECK120012172
ECK120012237
ECK120012280
ECK120012304
ECK120012587
ECK120012683
ECK120012694
ECK120012696
ECK120012808
ECK120012818
ECK120012820
ECK120012911
ECK120013104
ECK120013106
ECK120013108
ECK120013308
ECK120013310
ECK120013355
ECK120013357
ECK120013431
ECK120013527
ECK120013657
ECK120013674
ECK120013690
ECK120013692
ECK120013694
ECK120013717
ECK120013725
ECK120013864
ECK120013869
ECK120013908
ECK120013992
ECK120014001
ECK120014024
ECK120014026
ECK120014059
ECK120014092
ECK120014158
ECK120014165
ECK120015610
ECK120015751
ECK120016208
ECK120016211
ECK120016213
ECK120017032
ECK120017039
ECK120020662
ECK120020665
ECK120020667
ECK120020669
ECK120020671
ECK120020673
ECK120020675
ECK120020677
ECK120020679
ECK120020681
ECK120020684
ECK120020686
ECK120020688
ECK120020690
ECK120020710
ECK120023162
ECK120023165
ECK120023167
ECK120031751
ECK120034556
ECK120051410
ECK120051412
ECK120051414
ECK120051416
ECK120051418
ECK125108733
ECK125110187
ECK125141262
Publications: Korner H., Sofia HJ., Zumft WG. Phylogeny of the bacterial superfamily of Crp-Fnr transcription regulators: exploiting the metabolic spectrum by controlling alternative gene programs. FEMS Microbiol Rev. 27(5):559-92 (2003). [Pubmed]

Lee DJ., Wing HJ., Savery NJ., Busby SJ. Analysis of interactions between Activating Region 1 of Escherichia coli FNR protein and the C-terminal domain of the RNA polymerase alpha subunit: use of alanine scanning and suppression genetics. Mol Microbiol. 37(5):1032-40 (2000). [Pubmed]

Blake T., Barnard A., Busby SJ., Green J. Transcription activation by FNR: evidence for a functional activating region 2. J Bacteriol. 184(21):5855-61 (2002). [Pubmed]

Lamberg KE., Luther C., Weber KD., Kiley PJ. Characterization of activating region 3 from Escherichia coli FNR. J Mol Biol. 315(3):275-83 (2002). [Pubmed]

Green J., Sharrocks AD., Green B., Geisow M., Guest JR. Properties of FNR proteins substituted at each of the five cysteine residues. Mol Microbiol. 8(1):61-8 (1993). [Pubmed]

Mettert EL., Kiley PJ. Contributions of [4Fe-4S]-FNR and integration host factor to fnr transcriptional regulation. J Bacteriol. 189(8):3036-43 (2007). [Pubmed]

Lambden PR., Guest JR. Mutants of Escherichia coli K12 unable to use fumarate as an anaerobic electron acceptor. J Gen Microbiol. 97(2):145-60 (1976). [Pubmed]

Shan Y., Pan Q., Liu J., Huang F., Sun H., Nishino K., Yan A. Covalently linking the Escherichia coli global anaerobic regulator FNR in tandem allows it to function as an oxygen stable dimer. Biochem Biophys Res Commun. 419(1):43-8 (2012). [Pubmed]

Crack JC., Le Brun NE., Thomson AJ., Green J., Jervis AJ. Reactions of nitric oxide and oxygen with the regulator of fumarate and nitrate reduction, a global transcriptional regulator, during anaerobic growth of Escherichia coli. Methods Enzymol. 437:191-209 (2008). [Pubmed]

Kiley PJ., Beinert H. Oxygen sensing by the global regulator, FNR: the role of the iron-sulfur cluster. FEMS Microbiol Rev. 22(5):341-52 (1998). [Pubmed]

Unden G., Achebach S., Holighaus G., Tran HG., Wackwitz B., Zeuner Y. Control of FNR function of Escherichia coli by O2 and reducing conditions. J Mol Microbiol Biotechnol. 4(3):263-8 (2002). [Pubmed]

Green J., Crack JC., Thomson AJ., LeBrun NE. Bacterial sensors of oxygen. Curr Opin Microbiol. 12(2):145-51 (2009). [Pubmed]

Scott C., Partridge JD., Stephenson JR., Green J. DNA target sequence and FNR-dependent gene expression. FEBS Lett. 541(1-3):97-101 (2003). [Pubmed]

Wing HJ., Williams SM., Busby SJ. Spacing requirements for transcription activation by Escherichia coli FNR protein. J Bacteriol. 177(23):6704-10 (1995). [Pubmed]

Spiro S., Gaston KL., Bell AI., Roberts RE., Busby SJ., Guest JR. Interconversion of the DNA-binding specificities of two related transcription regulators, CRP and FNR. Mol Microbiol. 4(11):1831-8 (1990). [Pubmed]

Eiglmeier K., Honore N., Iuchi S., Lin EC., Cole ST. Molecular genetic analysis of FNR-dependent promoters. Mol Microbiol. 3(7):869-78 (1989). [Pubmed]

Gerasimova AV., Rodionov DA., Mironov AA., Gel'fand MS. [Computer analysis of regulatory signals in bacterial genomes. Fnr binding segments] Mol Biol (Mosk). 35(6):1001-9 (2001). [Pubmed]

Mettert EL., Kiley PJ. ClpXP-dependent proteolysis of FNR upon loss of its O2-sensing [4Fe-4S] cluster. J Mol Biol. 354(2):220-32 (2005). [Pubmed]

Cruz-Ramos H., Crack J., Wu G., Hughes MN., Scott C., Thomson AJ., Green J., Poole RK. NO sensing by FNR: regulation of the Escherichia coli NO-detoxifying flavohaemoglobin, Hmp. EMBO J. 21(13):3235-44 (2002). [Pubmed]

Sutton VR., Stubna A., Patschkowski T., Munck E., Beinert H., Kiley PJ. Superoxide destroys the [2Fe-2S]2+ cluster of FNR from Escherichia coli. Biochemistry. 43(3):791-8 (2004). [Pubmed]

Reinhart F., Achebach S., Koch T., Unden G. Reduced apo-fumarate nitrate reductase regulator (apoFNR) as the major form of FNR in aerobically growing Escherichia coli. J Bacteriol. 190(3):879-86 (2008). [Pubmed]

Lazazzera BA., Beinert H., Khoroshilova N., Kennedy MC., Kiley PJ. DNA binding and dimerization of the Fe-S-containing FNR protein from Escherichia coli are regulated by oxygen. J Biol Chem. 271(5):2762-8 (1996). [Pubmed]

Khoroshilova N., Popescu C., Munck E., Beinert H., Kiley PJ. Iron-sulfur cluster disassembly in the FNR protein of Escherichia coli by O2: [4Fe-4S] to [2Fe-2S] conversion with loss of biological activity. Proc Natl Acad Sci U S A. 94(12):6087-92 (1997). [Pubmed]

Jervis AJ., Crack JC., White G., Artymiuk PJ., Cheesman MR., Thomson AJ., Le Brun NE., Green J. The O2 sensitivity of the transcription factor FNR is controlled by Ser24 modulating the kinetics of [4Fe-4S] to [2Fe-2S] conversion. Proc Natl Acad Sci U S A. 106(12):4659-64 (2009). [Pubmed]

Yan A., Kiley PJ. Techniques to isolate O2-sensitive proteins: [4Fe-4S]-FNR as an example. Methods Enzymol. 463:787-805 (2009). [Pubmed]

Moore LJ., Kiley PJ. Characterization of the dimerization domain in the FNR transcription factor. J Biol Chem. 276(49):45744-50 (2001). [Pubmed]

Sutton VR., Mettert EL., Beinert H., Kiley PJ. Kinetic analysis of the oxidative conversion of the [4Fe-4S]2+ cluster of FNR to a [2Fe-2S]2+ Cluster. J Bacteriol. 186(23):8018-25 (2004). [Pubmed]

Salmon K., Hung SP., Mekjian K., Baldi P., Hatfield GW., Gunsalus RP. Global gene expression profiling in Escherichia coli K12. The effects of oxygen availability and FNR. J Biol Chem. 278(32):29837-55 (2003). [Pubmed]

Kang Y., Weber KD., Qiu Y., Kiley PJ., Blattner FR. Genome-wide expression analysis indicates that FNR of Escherichia coli K-12 regulates a large number of genes of unknown function. J Bacteriol. 187(3):1135-60 (2005). [Pubmed]
Related annotations: PaperBLAST

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