Transcription Factor
| Accessions: | ECK120007897 (RegulonDB 7.5) |
| Names: | DgsA, DgsA DNA-binding transcriptional repressor |
| 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: | DgsA, better known as Mlc, makes large colonies, Hosono K,1995is a transcriptional dualregulator that controls the expression of a number of genes encoding enzymes of the Escherichia coliphosphotransferase (PTS) and phosphoenolpyruvate (PEP) systems Plumbridge J.,2002; Pradhanang V,2005 It also regulates genesinvolved in the uptake of glucose Plumbridge J.,2001 It is considered a global regulator of carbohydrate metabolismDecker K,1998; Kimata K,1998; In addition, Mlc regulates expression of the MalT transcriptional regulator, the activator of themaltose regulon Decker K,1998; Mlc repressor function is disabled by binding of Mlc to an actively-transported and dephosphorylated form of PtsG(EIICBGlc) Lee SJ,2000; Nam TW,2001 The membrane-bound part of EIICBGlc is essential forMlc inactivation Nam TW,2001; Seitz S,2003; Analysis of the crystal structures of the tetrameric Mlc/EIIB complex shows amolecular mechanism of Mlc inactivation by membrane sequestration, in which Mlc loss its DNA binding ability in vivodue to the conformational obstruction by EIIB molecules Nam TW,2008The crystal structure of Mlc has been determined Gerber K,2005; Schiefner A,2005to 2.85 and 2.7 Å resolution and Mlc incomplex with four molecules of enzyme IIBGlc (EIIB) Nam TW,2008 to 2.85 Å resolution; Mlc forms stable dimersand binds to palindromic operator sites; The N-terminal region has a helix-turn-helix domain, and a C-terminal helix is implicated in EIICBGlc binding Seitz S,2003; Mlc forms tetramers in solution Gerber K,2005; Nam TW,2001 The Mlc monomer is composed of three domains: a DNA-binding motif (D-domain), an EIICBGlc-binding motif (E-domain), and an oligomerization domain (O-domain) Nam TW,2008.Mlc is autoregulated Decker K,1998; Shin D,2001 but it is also repressed and activated by CRP Shin D,2001 Mlc binds to sites with a length of 23 bp; Its consensus sequence has been determined Plumbridge J.,2001The intracellular concentration of Mlc is very limited Nam TW,2001 Zinc mediates the Mlc repressor function Schiefner A,2005 Mlc has a high homology with the NagC transcriptional dual regulator (40% identity and 80% similarity) Hosono K,1995; Cho S,2005 At the post-transcriptional level, Mlc interacts with MtfA, which is involved in the regulation of the ptsG Becker AK,2006Mlc is a member of the ROK (repressor, ORFs, kinases) (NagC/XylR) family of proteins, which contains at least two distinct classes of proteins: xylose repressor (XylR) and a series of glucose/fructose kinases Titgemeyer F,1994; Hansen T,2002.; global; repressor; operon; Transcription related; cytoplasmic polysaccharides; polysaccharide biosynthetic process; metal ion binding; carbohydrate metabolic process; DNA binding; transcription, DNA-dependent; cytoplasm |
| Length: | 407 |
| Pfam Domains: | 92-273 ROK family |
| Sequence: (in bold interface residues) | 1 VVAENQPGHIDQIKQTNAGAVYRLIDQLGPVSRIDLSRLAQLAPASITKIVREMLEAHLV 60 61 QELEIKEAGNRGRPAVGLVVETEAWHYLSLRISRGEIFLALRDLSSKLVVEESQELALKD 120 121 DLPLLDRIISHIDQFFIRHQKKLERLTSIAITLPGIIDTENGIVHRMPFYEDVKEMPLGE 180 181 ALEQHTGVPVYIQHDISAWTMAEALFGASRGARDVIQVVIDHNVGAGVITDGHLLHAGSS 240 241 SLVEIGHTQVDPYGKRCYCGNHGCLETIASVDSILELAQLRLNQSMSSMLHGQPLTVDSL 300 301 CQAALRGDLLAKDIITGVGAHVGRILAIMVNLFNPQKILIGSPLSKAADILFPVISDSIR 360 361 QQALPAYSQHISVESTQFSNQGTMAGAALVKDAMYNGSLLIRLLQG* |
| Interface Residues: | 10, 44, 45, 46, 48, 49, 74 |
| 3D-footprint Homologues: | 5f7q_C |
| Binding Motifs: | DgsA TTWTTTTrvwbykCGwAAWWAwT |
| Binding Sites: | ECK120011242 ECK120011244 ECK120013416 ECK120014107 ECK120014113 ECK120015755 |
| Publications: | Plumbridge J. DNA binding sites for the Mlc and NagC proteins: regulation of nagE, encoding the N-acetylglucosamine-specific transporter in Escherichia coli. Nucleic Acids Res. 29(2):506-14 (2001). [Pubmed] Titgemeyer F., Reizer J., Reizer A., Saier MH. Evolutionary relationships between sugar kinases and transcriptional repressors in bacteria. Microbiology. 140 ( Pt 9):2349-54 (1994). [Pubmed] Hansen T., Reichstein B., Schmid R., Schonheit P. The first archaeal ATP-dependent glucokinase, from the hyperthermophilic crenarchaeon Aeropyrum pernix, represents a monomeric, extremely thermophilic ROK glucokinase with broad hexose specificity. J Bacteriol. 184(21):5955-65 (2002). [Pubmed] Cho S., Shin D., Ji GE., Heu S., Ryu S. High-level recombinant protein production by overexpression of Mlc in Escherichia coli. J Biotechnol. 119(2):197-203 (2005). [Pubmed] Shin D., Lim S., Seok YJ., Ryu S. Heat shock RNA polymerase (E sigma(32)) is involved in the transcription of mlc and crucial for induction of the Mlc regulon by glucose in Escherichia coli. J Biol Chem. 276(28):25871-5 (2001). [Pubmed] Schiefner A., Gerber K., Seitz S., Welte W., Diederichs K., Boos W. The crystal structure of Mlc, a global regulator of sugar metabolism in Escherichia coli. J Biol Chem. 280(32):29073-9 (2005). [Pubmed] Gerber K., Boos W., Welte W., Schiefner A. Crystallization and preliminary X-ray analysis of Mlc from Escherichia coli. Acta Crystallogr Sect F Struct Biol Cryst Commun. 61(Pt 2):183-5 (2005). [Pubmed] Nam TW., Jung HI., An YJ., Park YH., Lee SH., Seok YJ., Cha SS. Analyses of Mlc-IIBGlc interaction and a plausible molecular mechanism of Mlc inactivation by membrane sequestration. Proc Natl Acad Sci U S A. 105(10):3751-6 (2008). [Pubmed] Seitz S., Lee SJ., Pennetier C., Boos W., Plumbridge J. Analysis of the interaction between the global regulator Mlc and EIIBGlc of the glucose-specific phosphotransferase system in Escherichia coli. J Biol Chem. 278(12):10744-51 (2003). [Pubmed] Nam TW., Cho SH., Shin D., Kim JH., Jeong JY., Lee JH., Roe JH., Peterkofsky A., Kang SO., Ryu S., Seok YJ. The Escherichia coli glucose transporter enzyme IICB(Glc) recruits the global repressor Mlc. EMBO J. 20(3):491-8 (2001). [Pubmed] Lee SJ., Boos W., Bouche JP., Plumbridge J. Signal transduction between a membrane-bound transporter, PtsG, and a soluble transcription factor, Mlc, of Escherichia coli. EMBO J. 19(20):5353-61 (2000). [Pubmed] Kimata K., Inada T., Tagami H., Aiba H. A global repressor (Mlc) is involved in glucose induction of the ptsG gene encoding major glucose transporter in Escherichia coli. Mol Microbiol. 29(6):1509-19 (1998). [Pubmed] Decker K., Plumbridge J., Boos W. Negative transcriptional regulation of a positive regulator: the expression of malT, encoding the transcriptional activator of the maltose regulon of Escherichia coli, is negatively controlled by Mlc. Mol Microbiol. 27(2):381-90 (1998). [Pubmed] Hosono K., Kakuda H., Ichihara S. Decreasing accumulation of acetate in a rich medium by Escherichia coli on introduction of genes on a multicopy plasmid. Biosci Biotechnol Biochem. 59(2):256-61 (1995). [Pubmed] Plumbridge J. Regulation of gene expression in the PTS in Escherichia coli: the role and interactions of Mlc. Curr Opin Microbiol. 5(2):187-93 (2002). [Pubmed] Pradhanang V., Ghimire S. Hirsutism: a rare presentation of an adult granulosa cell tumor of ovary. Nepal Med Coll J. 7(2):152-4 (2005). [Pubmed] Becker AK., Zeppenfeld T., Staab A., Seitz S., Boos W., Morita T., Aiba H., Mahr K., Titgemeyer F., Jahreis K. YeeI, a Novel Protein Involved in Modulation of the Activity of the Glucose-Phosphotransferase System in Escherichia coli K-12. J Bacteriol. 188(15):5439-49 (2006). [Pubmed] |
| Related annotations: | PaperBLAST |
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