Transcription Factor
| Accessions: | ECK120005002 (RegulonDB 7.5) |
| Names: | LexA |
| 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: | SOS response; transcription, DNA-dependent; repressor; regulon; Transcription related; cytoplasm; transcriptionally active chromatin; serine-type endopeptidase activity; regulation of transcription, DNA-dependent; hydrolase activity; response to DNA damage stimulus; proteolysis; DNA replication; DNA binding; DNA repair |
| Length: | 203 |
| Pfam Domains: | 1-65 LexA DNA binding domain 114-180 Peptidase S24-like |
| Sequence: (in bold interface residues) | 1 MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVIEIVS 60 61 GASRGIRLLQEEEEGLPLVGRVAAGEPLLAQQHIEGHYQVDPSLFKPNADFLLRVSGMSM 120 121 KDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNKVELLPENSEFKPIVVD 180 181 LRQQSFTIEGLAVGVIRNGDWL* |
| Interface Residues: | 28, 39, 40, 41, 42, 44, 45 |
| 3D-footprint Homologues: | 3jso_B |
| Binding Motifs: | LexA waCTGtATAwAwawmCAGya |
| Binding Sites: | ECK120012772 ECK120012774 ECK120012875 ECK120012890 ECK120012898 ECK120012901 ECK120012903 ECK120013419 ECK120013837 ECK120015229 ECK120015620 ECK120015626 ECK120015628 ECK120015705 ECK120015707 ECK120015709 ECK120015711 ECK120015767 ECK120015769 ECK120015969 ECK120016101 ECK120016106 ECK120016145 ECK120019269 ECK120019273 ECK120019275 ECK120033006 ECK120033008 ECK120033346 ECK120048800 ECK120048802 ECK120048804 ECK120048806 ECK120048810 ECK120048812 ECK120048814 ECK120051321 ECK120051386 ECK125108646 |
| Publications: | Luo Y., Pfuetzner RA., Mosimann S., Paetzel M., Frey EA., Cherney M., Kim B., Little JW., Strynadka NC. Crystal structure of LexA: a conformational switch for regulation of self-cleavage. Cell. 106(5):585-94 (2001). [Pubmed] Schnarr M., Granger-Schnarr M., Hurstel S., Pouyet J. The carboxy-terminal domain of the LexA repressor oligomerises essentially as the entire protein. FEBS Lett. 234(1):56-60 (1988). [Pubmed] Little JW., Mount DW., Yanisch-Perron CR. Purified lexA protein is a repressor of the recA and lexA genes. Proc Natl Acad Sci U S A. 78(7):4199-203 (1981). [Pubmed] Mohana-Borges R., Pacheco AB., Sousa FJ., Foguel D., Almeida DF., Silva JL. LexA repressor forms stable dimers in solution. The role of specific dna in tightening protein-protein interactions. J Biol Chem. 275(7):4708-12 (2000). [Pubmed] Erill I., Escribano M., Campoy S., Barbe J. In silico analysis reveals substantial variability in the gene contents of the gamma proteobacteria LexA-regulon. Bioinformatics. 19(17):2225-36 (2003). [Pubmed] Walker GC. Mutagenesis and inducible responses to deoxyribonucleic acid damage in Escherichia coli. Microbiol Rev. 48(1):60-93 (1984). [Pubmed] Gillor O., Vriezen JA., Riley MA. The role of SOS boxes in enteric bacteriocin regulation. Microbiology. 154(Pt 6):1783-92 (2008). [Pubmed] Zhang AP., Pigli YZ., Rice PA. Structure of the LexA-DNA complex and implications for SOS box measurement. Nature. 466(7308):883-6 (2010). [Pubmed] Krueger JH., Elledge SJ., Walker GC. Isolation and characterization of Tn5 insertion mutations in the lexA gene of Escherichia coli. J Bacteriol. 153(3):1368-78 (1983). [Pubmed] Brown MH., Paulsen IT., Skurray RA. The multidrug efflux protein NorM is a prototype of a new family of transporters. Mol Microbiol. 31(1):394-5 (1999). [Pubmed] Butala M., Zgur-Bertok D., Busby SJ. The bacterial LexA transcriptional repressor. Cell Mol Life Sci. 66(1):82-93 (2009). [Pubmed] d'Ari R. The SOS system. Biochimie. 67(3-4):343-7 (1985). [Pubmed] Fernandez De Henestrosa AR., Ogi T., Aoyagi S., Chafin D., Hayes JJ., Ohmori H., Woodgate R. Identification of additional genes belonging to the LexA regulon in Escherichia coli. Mol Microbiol. 35(6):1560-72 (2000). [Pubmed] Brent R., Ptashne M. The lexA gene product represses its own promoter. Proc Natl Acad Sci U S A. 77(4):1932-6 (1980). [Pubmed] Chen Z., Yang H., Pavletich NP. Mechanism of homologous recombination from the RecA-ssDNA/dsDNA structures. Nature. 453(7194):489-4 (2008). [Pubmed] Cox MM. Regulation of bacterial RecA protein function. Crit Rev Biochem Mol Biol. 42(1):41-63 (2007). [Pubmed] Giese KC., Michalowski CB., Little JW. RecA-dependent cleavage of LexA dimers. J Mol Biol. 377(1):148-61 (2008). [Pubmed] Little JW. Mechanism of specific LexA cleavage: autodigestion and the role of RecA coprotease. Biochimie. 73(4):411-21 (1991). [Pubmed] Butala M., Klose D., Hodnik V., Rems A., Podlesek Z., Klare JP., Anderluh G., Busby SJ., Steinhoff HJ., Zgur-Bertok D. Interconversion between bound and free conformations of LexA orchestrates the bacterial SOS response. Nucleic Acids Res (2011). [Pubmed] Mazon G., Erill I., Campoy S., Cortes P., Forano E., Barbe J. Reconstruction of the evolutionary history of the LexA-binding sequence. Microbiology. 150(Pt 11):3783-95 (2004). [Pubmed] Fogh RH., Ottleben G., Ruterjans H., Schnarr M., Boelens R., Kaptein R. Solution structure of the LexA repressor DNA binding domain determined by 1H NMR spectroscopy. EMBO J. 13(17):3936-44 (1994). [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.