Transcription Factor
| Accessions: | ECK120005310 (RegulonDB 7.5) |
| Names: | RhaS |
| 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: | DNA binding; sequence-specific DNA binding transcription factor activity; intracellular; rhamnose metabolic process; sequence-specific DNA binding; regulation of transcription, DNA-dependent; cytoplasm; Transcription related; activator; operon; carbon compounds; transcription, DNA-dependent |
| Length: | 279 |
| Pfam Domains: | 16-154 AraC-like ligand binding domain 180-221 Bacterial regulatory helix-turn-helix proteins, AraC family 193-271 Helix-turn-helix domain 232-271 Bacterial regulatory helix-turn-helix proteins, AraC family |
| Sequence: (in bold interface residues) | 1 MTVLHSVDFFPSGNASVAIEPRLPQADFPEHHHDFHEIVIVEHGTGIHVFNGQPYTITGG 60 61 TVCFVRDHDRHLYEHTDNLCLTNVLYRSPDRFQFLAGLNQLLPQELDGQYPSHWRVNHSV 120 121 LQQVRQLVAQMEQQEGENDLPSTASREILFMQLLLLLRKSSLQENLENSASRLNLLLAWL 180 181 EDHFADEVNWDAVADQFSLSLRTLHRQLKQQTGLTPQRYLNRLRLMKARHLLRHSEASVT 240 241 DIAYRCGFSDSNHFSTLFRREFNWSPRDIRQGRDGFLQ* |
| Interface Residues: | 200, 201, 202, 203, 205, 206, 209, 217, 251, 252, 255, 256, 260 |
| 3D-footprint Homologues: | 3w6v_A, 7vwz_G, 1xs9_A, 1zgw_A |
| Binding Motifs: | RhaS TtrmamtyTCsmCgkTw |
| Binding Sites: | ECK120012339 ECK120013235 ECK120013279 ECK120013285 ECK125108625 ECK125141916 ECK125141918 |
| Publications: | Wickstrum JR., Santangelo TJ., Egan SM. Cyclic AMP receptor protein and RhaR synergistically activate transcription from the L-rhamnose-responsive rhaSR promoter in Escherichia coli. J Bacteriol. 187(19):6708-18 (2005). [Pubmed] Holcroft CC., Egan SM. Roles of cyclic AMP receptor protein and the carboxyl-terminal domain of the alpha subunit in transcription activation of the Escherichia coli rhaBAD operon. J Bacteriol. 182(12):3529-35 (2000). [Pubmed] Bhende PM., Egan SM. Amino acid-DNA contacts by RhaS: an AraC family transcription activator. J Bacteriol. 181(17):5185-92 (1999). [Pubmed] Kolin A., Jevtic V., Swint-Kruse L., Egan SM. Linker regions of the RhaS and RhaR proteins. J Bacteriol. 189(1):269-71 (2007). [Pubmed] Wickstrum JR., Egan SM. Amino acid contacts between sigma 70 domain 4 and the transcription activators RhaS and RhaR. J Bacteriol. 186(18):6277-85 (2004). [Pubmed] Via P., Badia J., Baldoma L., Obradors N., Aguilar J. Transcriptional regulation of the Escherichia coli rhaT gene. Microbiology. 142 ( Pt 7):1833-40 (1996). [Pubmed] Egan SM., Schleif RF. A regulatory cascade in the induction of rhaBAD. J Mol Biol. 234(1):87-98 (1993). [Pubmed] Wickstrum JR., Skredenske JM., Kolin A., Jin DJ., Fang J., Egan SM. Transcription activation by the DNA-binding domain of the AraC family protein RhaS in the absence of its effector-binding domain. J Bacteriol. 189(14):4984-93 (2007). [Pubmed] Bhende PM., Egan SM. Genetic evidence that transcription activation by RhaS involves specific amino acid contacts with sigma 70. J Bacteriol. 182(17):4959-69 (2000). [Pubmed] Egan SM., Schleif RF. DNA-dependent renaturation of an insoluble DNA binding protein. Identification of the RhaS binding site at rhaBAD. J Mol Biol. 243(5):821-9 (1994). [Pubmed] Kolin A., Balasubramaniam V., Skredenske JM., Wickstrum JR., Egan SM. Differences in the mechanism of the allosteric l-rhamnose responses of the AraC/XylS family transcription activators RhaS and RhaR. Mol Microbiol. 68(2):448-61 (2008). [Pubmed] |
| Related annotations: | PaperBLAST |
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