Transcription Factor
| Accessions: | ECK120007927 (RegulonDB 7.5) |
| Names: | SlyA, SlyA DNA-binding transcriptional activator |
| 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: | SlyA (for hemolytic protein in Salmonella) was initially identified in Salmonella, although little is known about the regulator role of SlyA; It has been demonstrated that SlyA increases expression of hemolysin E by antagonizing the negative effects of H-NS Ludwig A,1999; Wyborn NR,2004 SlyA belongs to the MarR family of transcriptional regulators; This protein consist of two domains, an amino-terminal domain involved in dimerization and a carboxy-terminal domain indispensable for DNA recognition Wu RY,2003 It is known that SlyA recognizes a short palindromic DNA sequence of 12 bp Wyborn NR,2004; pathogenesis; regulation of transcription, DNA-dependent; cytoplasm; Transcription related; activator; operon; cell killing; intracellular; transcription activator activity; transcription, DNA-dependent; DNA binding; sequence-specific DNA binding transcription factor activity |
| Length: | 145 |
| Pfam Domains: | 28-87 MarR family 29-87 MarR family 29-95 Winged helix DNA-binding domain |
| Sequence: (in bold interface residues) | 1 LESPLGSDLARLVRIWRALIDHRLKPLELTQTHWVTLHNIHQLPPDQSQIQLAKAIGIEQ 60 61 PSLVRTLDQLEEKGLISRQTCASDRRAKRIKLTEKAEPLISEMEAVINKTRAEILHGISA 120 121 EELEQLITLIAKLEHNIIELQAKG* |
| Interface Residues: | 49, 59, 60, 61, 62, 64, 65, 66, 68, 69, 85, 86 |
| 3D-footprint Homologues: | 7el3_B, 7pza_B, 5yi2_J, 7bhy_A, 5h3r_A, 1z9c_A, 6c2s_C, 3q5f_A, 6jbx_A, 4aik_A, 4fx4_B, 5hlg_E, 4kdp_B, 3zpl_B, 6q2b_B, 5f7q_C, 5hso_A, 7dvv_A |
| Binding Motifs: | SlyA ATawTtAmAGA |
| Binding Sites: | ECK120012255 ECK120014028 ECK120033896 ECK120033898 ECK120033900 ECK120033902 |
| Publications: | Wyborn NR., Stapleton MR., Norte VA., Roberts RE., Grafton J., Green J. Regulation of Escherichia coli hemolysin E expression by H-NS and Salmonella SlyA. J Bacteriol. 186(6):1620-8 (2004). [Pubmed] Ludwig A., Bauer S., Benz R., Bergmann B., Goebel W. Analysis of the SlyA-controlled expression, subcellular localization and pore-forming activity of a 34 kDa haemolysin (ClyA) from Escherichia coli K-12. Mol Microbiol. 31(2):557-67 (1999). [Pubmed] Wu RY., Zhang RG., Zagnitko O., Dementieva I., Maltzev N., Watson JD., Laskowski R., Gornicki P., Joachimiak A. Crystal structure of Enterococcus faecalis SlyA-like transcriptional factor. J Biol Chem. 278(22):20240-4 (2003). [Pubmed] |
| Related annotations: | PaperBLAST |
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