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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