Transcription Factor
| Accessions: | ECK120004542 (RegulonDB 7.5) |
| Names: | ArgR |
| 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; arginine; activator; repressor; cytoplasm; transcription, DNA-dependent; arginine biosynthetic process; DNA binding; sequence-specific DNA binding transcription factor activity; regulation of transcription, DNA-dependent; cellular amino acid biosynthetic process; plasmid recombination; transcription regulatory region DNA binding; negative regulation of transcription initiation, DNA-dependent |
| Length: | 157 |
| Pfam Domains: | 6-74 Arginine repressor, DNA binding domain 82-150 Arginine repressor, C-terminal domain |
| Sequence: (in bold interface residues) | 1 MRSSAKQEELVKAFKALLKEEKFSSQGEIVAALQEQGFDNINQSKVSRMLTKFGAVRTRN 60 61 AKMEMVYCLPAELGVPTTSSPLKNLVLDIDYNDAVVVIHTSPGAAQLIARLLDSLGKAEG 120 121 ILGTIAGDDTIFTTPANGFTVKDLYEAILELFDQEL* |
| Interface Residues: | 42, 43, 44, 47, 48 |
| 3D-footprint Homologues: | 3lap_B |
| Binding Motifs: | ArgR hwArTGAATwwThATkCA |
| Binding Sites: | ECK120011673 ECK120011675 ECK120011677 ECK120011679 ECK120012260 ECK120012263 ECK120012266 ECK120012608 ECK120012611 ECK120012614 ECK120012616 ECK120012618 ECK120012620 ECK120012622 ECK120012624 ECK120012652 ECK120012654 ECK120020708 ECK120020769 ECK120029619 ECK120029620 ECK120032395 ECK120032397 ECK120033152 ECK120033342 ECK120033343 ECK120033344 |
| Publications: | Kiupakis AK., Reitzer L. ArgR-independent induction and ArgR-dependent superinduction of the astCADBE operon in Escherichia coli. J Bacteriol. 184(11):2940-50 (2002). [Pubmed] Makarova KS., Mironov AA., Gelfand MS. Conservation of the binding site for the arginine repressor in all bacterial lineages. Genome Biol. 2(4):RESEARCH0013 (2001). [Pubmed] Tian G., Lim D., Carey J., Maas WK. Binding of the arginine repressor of Escherichia coli K12 to its operator sites. J Mol Biol. 226(2):387-97 (1992). [Pubmed] Caldara M., Minh PN., Bostoen S., Massant J., Charlier D. ArgR-dependent Repression of Arginine and Histidine Transport Genes in Escherichia coli K-12. J Mol Biol. 373(2):251-67 (2007). [Pubmed] Sunnerhagen M., Nilges M., Otting G., Carey J. Solution structure of the DNA-binding domain and model for the complex of multifunctional hexameric arginine repressor with DNA. Nat Struct Biol. 4(10):819-26 (1997). [Pubmed] Senechal H., Delesques J., Szatmari G. Escherichia coli ArgR mutants defective in cer/Xer recombination, but not in DNA binding. FEMS Microbiol Lett. 305(2):162-9 (2010). [Pubmed] Jin L., Xue WF., Fukayama JW., Yetter J., Pickering M., Carey J. Asymmetric allosteric activation of the symmetric ArgR hexamer. J Mol Biol. 346(1):43-56 (2005). [Pubmed] Lim DB., Oppenheim JD., Eckhardt T., Maas WK. Nucleotide sequence of the argR gene of Escherichia coli K-12 and isolation of its product, the arginine repressor. Proc Natl Acad Sci U S A. 84(19):6697-701 (1987). [Pubmed] Charlier D., Roovers M., Van Vliet F., Boyen A., Cunin R., Nakamura Y., Glansdorff N., Pierard A. Arginine regulon of Escherichia coli K-12. A study of repressor-operator interactions and of in vitro binding affinities versus in vivo repression. J Mol Biol. 226(2):367-86 (1992). [Pubmed] Stirling CJ., Szatmari G., Stewart G., Smith MC., Sherratt DJ. The arginine repressor is essential for plasmid-stabilizing site-specific recombination at the ColE1 cer locus. EMBO J. 7(13):4389-95 (1988). [Pubmed] Van Duyne GD., Ghosh G., Maas WK., Sigler PB. Structure of the oligomerization and L-arginine binding domain of the arginine repressor of Escherichia coli. J Mol Biol. 256(2):377-91 (1996). [Pubmed] Caldara M., Charlier D., Cunin R. The arginine regulon of Escherichia coli: whole-system transcriptome analysis discovers new genes and provides an integrated view of arginine regulation. Microbiology. 152(Pt 11):3343-54 (2006). [Pubmed] |
| Related annotations: | PaperBLAST |
Disclaimer and license
These data are available AS IS and at your own risk. The EEAD/CSIC do not give any representation or warranty nor assume any liability or responsibility for the data nor the results posted (whether as to their accuracy, completeness, quality or otherwise). Access to these data is available free of charge for ordinary use in the course of research. Downloaded data have CC-BY-NC-SA license. FootprintDB is also available at RSAT::Plants, part of the INB/ELIXIR-ES resources portfolio.