Transcription Factor
| Accessions: | ECK120004771 (RegulonDB 7.5) |
| Names: | FhlA, FhlA 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: | transcription factor binding; regulation of transcription, DNA-dependent; intracellular; ATP binding; sequence-specific DNA binding transcription factor activity; DNA binding; nucleotide binding; two-component signal transduction system (phosphorelay); transcription, DNA-dependent; fermentation; operon; activator; Transcription related; cytoplasm; nucleoside-triphosphatase activity |
| Length: | 693 |
| Pfam Domains: | 202-344 GAF domain 202-345 GAF domain 202-346 GAF domain 381-548 Sigma-54 interaction domain 405-529 AAA domain (dynein-related subfamily) 405-525 ATPase family associated with various cellular activities (AAA) 645-684 Bacterial regulatory protein, Fis family |
| Sequence: (in bold interface residues) | 1 MSYTPMSDLGQQGLFDITRTLLQQPDLASLCEALSQLVKRSALADNAAIVLWQAQTQRAS 60 61 YYASREKDTPIKYEDETVLAHGPVRSILSRPDTLHCSYEEFCETWPQLDAGGLYPKFGHY 120 121 CLMPLAAEGHIFGGCEFIRYDDRPWSEKEFNRLQTFTQIVSVVTEQIQSRVVNNVDYELL 180 181 CRERDNFRILVAITNAVLSRLDMDELVSEVAKEIHYYFDIDDISIVLRSHRKNKLNIYST 240 241 HYLDKQHPAHEQSEVDEAGTLTERVFKSKEMLLINLHERDDLAPYERMLFDTWGNQIQTL 300 301 CLLPLMSGDTMLGVLKLAQCEEKVFTTTNLNLLRQIAERVAIAVDNALAYQEIHRLKERL 360 361 VDENLALTEQLNNVDSEFGEIIGRSEAMYSVLKQVEMVAQSDSTVLILGETGTGKELIAR 420 421 AIHNLSGRNNRRMVKMNCAAMPAGLLESDLFGHERGAFTGASAQRIGRFELADKSSLFLD 480 481 EVGDMPLELQPKLLRVLQEQEFERLGSNKIIQTDVRLIAATNRDLKKMVADREFRSDLYY 540 541 RLNVFPIHLPPLRERPEDIPLLAKAFTFKIARRLGRNIDSIPAETLRTLSNMEWPGNVRE 600 601 LENVIERAVLLTRGNVLQLSLPDIVLPEPETPPAATVVALEGEDEYQLIVRVLKETNGVV 660 661 AGPKGAAQRLGLKRTTLLSRMKRLGIDKSALI* |
| Interface Residues: | 448, 453, 454, 455 |
| 3D-footprint Homologues: | 5fhd_A, 8eaf_A |
| Binding Motifs: | FhlA YGKCRAmAmkGmcr |
| Binding Sites: | ECK120011396 ECK120013095 ECK120013097 ECK120013099 ECK125109813 ECK125109814 ECK125109815 |
| Publications: | Iuchi S., Lin EC. Adaptation of Escherichia coli to redox environments by gene expression. Mol Microbiol. 9(1):9-15 (1993). [Pubmed] Andrews SC., Berks BC., McClay J., Ambler A., Quail MA., Golby P., Guest JR. A 12-cistron Escherichia coli operon (hyf) encoding a putative proton-translocating formate hydrogenlyase system. Microbiology. 143 ( Pt 11):3633-47 (1997). [Pubmed] Self WT., Hasona A., Shanmugam KT. Expression and regulation of a silent operon, hyf, coding for hydrogenase 4 isoenzyme in Escherichia coli. J Bacteriol. 186(2):580-7 (2004). [Pubmed] Maupin JA., Shanmugam KT. Genetic regulation of formate hydrogenlyase of Escherichia coli: role of the fhlA gene product as a transcriptional activator for a new regulatory gene, fhlB. J Bacteriol. 172(9):4798-806 (1990). [Pubmed] Sankar P., Lee JH., Shanmugam KT. Gene-product relationships of fhlA and fdv genes of Escherichia coli. J Bacteriol. 170(12):5440-5 (1988). [Pubmed] Schlensog V., Bock A. Identification and sequence analysis of the gene encoding the transcriptional activator of the formate hydrogenlyase system of Escherichia coli. Mol Microbiol. 4(8):1319-27 (1990). [Pubmed] Rossmann R., Sawers G., Bock A. Mechanism of regulation of the formate-hydrogenlyase pathway by oxygen, nitrate, and pH: definition of the formate regulon. Mol Microbiol. 5(11):2807-14 (1991). [Pubmed] Hopper S., Babst M., Schlensog V., Fischer HM., Hennecke H., Bock A. Regulated expression in vitro of genes coding for formate hydrogenlyase components of Escherichia coli. J Biol Chem. 269(30):19597-604 (1994). [Pubmed] Maeda T., Sanchez-Torres V., Wood TK. Enhanced hydrogen production from glucose by metabolically engineered Escherichia coli. Appl Microbiol Biotechnol. 77(4):879-90 (2007). [Pubmed] Maeda T., Sanchez-Torres V., Wood TK. Escherichia coli hydrogenase 3 is a reversible enzyme possessing hydrogen uptake and synthesis activities. Appl Microbiol Biotechnol. 76(5):1035-42 (2007). [Pubmed] Schlensog V., Lutz S., Bock A. Purification and DNA-binding properties of FHLA, the transcriptional activator of the formate hydrogenlyase system from Escherichia coli. J Biol Chem. 269(30):19590-6 (1994). [Pubmed] Sauter M., Bohm R., Bock A. Mutational analysis of the operon (hyc) determining hydrogenase 3 formation in Escherichia coli. Mol Microbiol. 6(11):1523-32 (1992). [Pubmed] Repoila F., Majdalani N., Gottesman S. Small non-coding RNAs, co-ordinators of adaptation processes in Escherichia coli: the RpoS paradigm. Mol Microbiol. 48(4):855-61 (2003). [Pubmed] Argaman L., Altuvia S. fhlA repression by OxyS RNA: kissing complex formation at two sites results in a stable antisense-target RNA complex. J Mol Biol. 300(5):1101-12 (2000). [Pubmed] Altuvia S., Zhang A., Argaman L., Tiwari A., Storz G. The Escherichia coli OxyS regulatory RNA represses fhlA translation by blocking ribosome binding. EMBO J. 17(20):6069-75 (1998). [Pubmed] Altuvia S., Weinstein-Fischer D., Zhang A., Postow L., Storz G. A small, stable RNA induced by oxidative stress: role as a pleiotropic regulator and antimutator. Cell. 90(1):43-53 (1997). [Pubmed] Self WT., Hasona A., Shanmugam KT. N-terminal truncations in the FhlA protein result in formate- and MoeA-independent expression of the hyc (formate hydrogenlyase) operon of Escherichia coli. Microbiology. 147(Pt 11):3093-104 (2001). [Pubmed] Hopper S., Bock A. Effector-mediated stimulation of ATPase activity by the sigma 54-dependent transcriptional activator FHLA from Escherichia coli. J Bacteriol. 177(10):2798-803 (1995). [Pubmed] Leonhartsberger S., Ehrenreich A., Bock A. Analysis of the domain structure and the DNA binding site of the transcriptional activator FhlA. Eur J Biochem. 267(12):3672-84 (2000). [Pubmed] Weiss DS., Batut J., Klose KE., Keener J., Kustu S. The phosphorylated form of the enhancer-binding protein NTRC has an ATPase activity that is essential for activation of transcription. Cell. 67(1):155-67 (1991). [Pubmed] Korsa I., Bock A. Characterization of fhlA mutations resulting in ligand-independent transcriptional activation and ATP hydrolysis. J Bacteriol. 179(1):41-5 (1997). [Pubmed] |
| Related annotations: | PaperBLAST |
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