Transcription Factor
| Accessions: | ECK120005031 (RegulonDB 7.5) |
| Names: | MalT, MalT 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: | cytoplasm; nucleotide binding; operon; activator; Transcription related; intracellular signal transduction; protein binding; trisaccharide binding; two-component response regulator activity; two-component signal transduction system (phosphorelay); sequence-specific DNA binding; regulation of transcription, DNA-dependent; transcription, DNA-dependent; carbohydrate metabolic process; intracellular; ATP binding; binding; sequence-specific DNA binding transcription factor activity; DNA binding; carbon compounds |
| Length: | 902 |
| Pfam Domains: | 834-890 Bacterial regulatory proteins, luxR family |
| Sequence: (in bold interface residues) | 1 MLIPSKLSRPVRLDHTVVRERLLAKLSGANNFRLALITSPAGYGKTTLISQWAAGKNDIG 60 61 WYSLDEGDNQQERFASYLIAAVQQATNGHCAICETMAQKRQYASLTSLFAQLFIELAEWH 120 121 SPLYLVIDDYHLITNPVIHESMRFFIRHQPENLTLVVLSRNLPQLGIANLRVRDQLLEIG 180 181 SQQLAFTHQEAKQFFDCRLSSPIEAAESSRICDDVSGWATALQLIALSARQNTHSAHKSA 240 241 RRLAGINASHLSDYLVDEVLDNVDLATRHFLLKSAILRSMNDALITRVTGEENGQMRLEE 300 301 IERQGLFLQRMDDTGEWFCYHPLFGNFLRQRCQWELAAELPEIHRAAAESWMAQGFPSEA 360 361 IHHALAAGDALMLRDILLNHAWSLFNHSELSLLEESLKALPWDSLLENPQLVLLQAWLMQ 420 421 SQHRYGEVNTLLARAEHEIKDIREDTMHAEFNALRAQVAINDGNPDEAERLAKLALEELP 480 481 PGWFYSRIVATSVLGEVLHCKGELTRSLALMQQTEQMARQHDVWHYALWSLIQQSEILFA 540 541 QGFLQTAWETQEKAFQLINEQHLEQLPMHEFLVRIRAQLLWAWARLDEAEASARSGIEVL 600 601 SSYQPQQQLQCLAMLIQCSLARGDLDNARSQLNRLENLLGNGKYHSDWISNANKVRVIYW 660 661 QMTGDKAAAANWLRHTAKPEFANNHFLQGQWRNIARAQILLGEFEPAEIVLEELNENARS 720 721 LRLMSDLNRNLLLLNQLYWQAGRKSDAQRVLLDALKLANRTGFISHFVIEGEAMAQQLRQ 780 781 LIQLNTLPELEQHRAQRILREINQHHRHKFAHFDENFVERLLNHPEVPELIRTSPLTQRE 840 841 WQVLGLIYSGYSNEQIAGELEVAATTIKTHIRNLYQKLGVAHRQDAVQHAQQLLKMMGYG 900 901 V* |
| Interface Residues: | 863, 865, 866, 868, 869, 870, 872, 873 |
| 3D-footprint Homologues: | 7ve5_B, 4wuh_B, 1je8_F, 1sax_A, 1zlk_A |
| Binding Motifs: | MalT srrGGakGAG |
| Binding Sites: | ECK120012221 ECK120012223 ECK120012225 ECK120012367 ECK120012369 ECK120012371 ECK120012381 ECK120012383 ECK120012460 ECK120012782 ECK120012785 ECK120012788 ECK120012790 ECK120013179 ECK120016486 |
| Publications: | Chapon C., Kolb A. Action of CAP on the malT promoter in vitro. J Bacteriol. 156(3):1135-43 (1983). [Pubmed] Eichenberger P., Dethiollaz S., Fujita N., Ishihama A., Geiselmann J. Influence of the location of the cAMP receptor protein binding site on the geometry of a transcriptional activation complex in Escherichia coli. Biochemistry. 35(48):15302-12 (1996). [Pubmed] Danot O., Raibaud O. Multiple protein-DNA and protein-protein interactions are involved in transcriptional activation by MalT. Mol Microbiol. 14(2):335-46 (1994). [Pubmed] Chapon C. Role of the catabolite activator protein in the maltose regulon of Escherichia coli. J Bacteriol. 150(2):722-9 (1982). [Pubmed] Schneider E., Freundlieb S., Tapio S., Boos W. Molecular characterization of the MalT-dependent periplasmic alpha-amylase of Escherichia coli encoded by malS. J Biol Chem. 267(8):5148-54 (1992). [Pubmed] Tapio S., Yeh F., Shuman HA., Boos W. The malZ gene of Escherichia coli, a member of the maltose regulon, encodes a maltodextrin glucosidase. J Biol Chem. 266(29):19450-8 (1991). [Pubmed] Boos W., Bohm A. Learning new tricks from an old dog: MalT of the Escherichia coli maltose system is part of a complex regulatory network. Trends Genet. 16(9):404-9 (2000). [Pubmed] Joly N., Bohm A., Boos W., Richet E. MalK, the ATP-binding Cassette Component of the Escherichia coli Maltodextrin Transporter, Inhibits the Transcriptional Activator MalT by Antagonizing Inducer Binding. J Biol Chem. 279(32):33123-30 (2004). [Pubmed] Schreiber V., Steegborn C., Clausen T., Boos W., Richet E. A new mechanism for the control of a prokaryotic transcriptional regulator: antagonistic binding of positive and negative effectors. Mol Microbiol. 35(4):765-76 (2000). [Pubmed] Joly N., Danot O., Schlegel A., Boos W., Richet E. The Aes protein directly controls the activity of MalT, the central transcriptional activator of the Escherichia coli maltose regulon. J Biol Chem. 277(19):16606-13 (2002). [Pubmed] Mandrich L., Caputo E., Martin BM., Rossi M., Manco G. The Aes protein and the monomeric alpha-galactosidase from Escherichia coli form a non-covalent complex. Implications for the regulation of carbohydrate metabolism. J Biol Chem. 277(50):48241-7 (2002). [Pubmed] Schlegel A., Danot O., Richet E., Ferenci T., Boos W. The N terminus of the Escherichia coli transcription activator MalT is the domain of interaction with MalY. J Bacteriol. 184(11):3069-77 (2002). [Pubmed] Dethiollaz S., Eichenberger P., Geiselmann J. Influence of DNA geometry on transcriptional activation in Escherichia coli. EMBO J. 15(19):5449-58 (1996). [Pubmed] Danot O. The inducer maltotriose binds in the central cavity of the tetratricopeptide-like sensor domain of MalT, a bacterial STAND transcription factor. Mol Microbiol. 77(3):628-41 (2010). [Pubmed] Ritzefeld M., Wollschlager K., Niemann G., Anselmetti D., Sewald N. Minor groove recognition is important for the transcription factor PhoB: a surface plasmon resonance study. Mol Biosyst. 7(11):3132-42 (2011). [Pubmed] Boos W., Shuman H. Maltose/maltodextrin system of Escherichia coli: transport, metabolism, and regulation. Microbiol Mol Biol Rev. 62(1):204-29 (1998). [Pubmed] Schlegel A., Bohm A., Lee SJ., Peist R., Decker K., Boos W. Network regulation of the Escherichia coli maltose system. J Mol Microbiol Biotechnol. 4(3):301-7 (2002). [Pubmed] Cole ST., Raibaud O. The nucleotide sequence of the malT gene encoding the positive regulator of the Escherichia coli maltose regulon. Gene. 42(2):201-8 (1986). [Pubmed] Richet E., Joly N., Danot O. Two domains of MalT, the activator of the Escherichia coli maltose regulon, bear determinants essential for anti-activation by MalK. J Mol Biol. 347(1):1-10 (2005). [Pubmed] Danot O. A complex signaling module governs the activity of MalT, the prototype of an emerging transactivator family. Proc Natl Acad Sci U S A. 98(2):435-40 (2001). [Pubmed] Steegborn C., Danot O., Huber R., Clausen T. Crystal structure of transcription factor MalT domain III: a novel helix repeat fold implicated in regulated oligomerization. Structure. 9(11):1051-60 (2001). [Pubmed] Vidal-Ingigliardi D., Richet E., Danot O., Raibaud O. A small C-terminal region of the Escherichia coli MalT protein contains the DNA-binding domain. J Biol Chem. 268(33):24527-30 (1993). [Pubmed] |
| Related annotations: | PaperBLAST |
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