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Escherichia coli K-12 substr. MG1655 Polypeptide: MalT transcriptional activator



Gene: malT Accession Numbers: EG10562 (EcoCyc), b3418, ECK3405

Synonyms: malA

Regulation Summary Diagram: ?

Component of:
MalT-MalK
MalT-Maltotriose-ATP DNA-binding transcriptional activator (extended summary available)

Citations: [Cole86, Richet89]

Gene Citations: [Kornacker89, Cole86]

Locations: cytosol

Map Position: [3,551,107 -> 3,553,812] (76.54 centisomes)
Length: 2706 bp / 901 aa

Molecular Weight of Polypeptide: 103.12 kD (from nucleotide sequence)

pI: 6.3

Unification Links: ASAP:ABE-0011162 , CGSC:526 , DIP:DIP-10149N , EchoBASE:EB0557 , EcoGene:EG10562 , EcoliWiki:b3418 , Mint:MINT-1233939 , ModBase:P06993 , OU-Microarray:b3418 , PortEco:malT , PR:PRO_000023155 , Pride:P06993 , Protein Model Portal:P06993 , RefSeq:NP_417877 , RegulonDB:EG10562 , SMR:P06993 , String:511145.b3418 , UniProt:P06993

Relationship Links: InterPro:IN-FAMILY:IPR000792 , InterPro:IN-FAMILY:IPR011990 , InterPro:IN-FAMILY:IPR011991 , InterPro:IN-FAMILY:IPR016032 , InterPro:IN-FAMILY:IPR023768 , InterPro:IN-FAMILY:IPR027417 , PDB:Structure:1HZ4 , Pfam:IN-FAMILY:PF00196 , Prints:IN-FAMILY:PR00038 , Prosite:IN-FAMILY:PS00622 , Prosite:IN-FAMILY:PS50043 , Smart:IN-FAMILY:SM00421

In Reactions of unknown directionality:

Not in pathways:
MalT + MalK = MalT-MalK
MalT + maltotriose + ATP = MalT-maltotriose-ATP

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0005975 - carbohydrate metabolic process Inferred by computational analysis [UniProtGOA11a]
GO:0006351 - transcription, DNA-templated Inferred by computational analysis [UniProtGOA11a]
GO:0006355 - regulation of transcription, DNA-templated Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0045893 - positive regulation of transcription, DNA-templated Inferred by computational analysis [GOA06]
GO:0045913 - positive regulation of carbohydrate metabolic process Inferred by computational analysis [GOA06]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Rajagopala14, Butland05, Joly02]
GO:0042802 - identical protein binding Inferred from experiment [Rajagopala14, Marquenet10]
GO:0048031 - trisaccharide binding Inferred from experiment [Danot10]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11a]
GO:0003677 - DNA binding Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01a]
GO:0003700 - sequence-specific DNA binding transcription factor activity Inferred by computational analysis [GOA06, GOA01a]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11a, GOA06]
Cellular Component: GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]

MultiFun Terms: information transfer RNA related Transcription related
metabolism carbon utilization carbon compounds
regulation genetic unit regulated operon
regulation type of regulation transcriptional level activator

DNA binding site length: 10 base-pairs

Essentiality data for malT knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Subunit of: MalT-MalK

Subunit composition of MalT-MalK = [MalT][MalK]
         MalT transcriptional activator = MalT
         maltose ABC transporter - ATP binding subunit = MalK (summary available)

In Reactions of unknown directionality:

Not in pathways:
MalT + MalK = MalT-MalK


Subunit of: MalT-Maltotriose-ATP DNA-binding transcriptional activator

Synonyms: MalA, B3418, MalT, MalT-maltotriose-ATP

Subunit composition of MalT-Maltotriose-ATP DNA-binding transcriptional activator = [MalT][maltotriose][ATP]
         MalT transcriptional activator = MalT

Summary:
The "Maltose regulator," MalT, is a transcription factor that activates transcription of several genes and operons involved in maltose catabolism and transport [Boos00, Tapio91, Schneider92, Chapon82, Danot94]. This regulator is sensitive to catabolite control and is induced when Escherichia coli is grown on maltodextrin in the absence of glucose [Chapon83, Eichenberger96, Dethiollaz96]. MalT is a STAND transcription factor, Signal Transduction ATP bases with numerous domains [Danot10][Liu13b]. A novel regulatory role for the MalT regulon in glycolysis-associated utilization of carbon sources has been identified [Ritzefeld11].

MalT is monomeric in solution, but in the presence of maltodextrin and ATP it forms multiple complexes (oligomers) in its target promoters and activates transcription by overlapping the -35 box of promoters [Schneider92, Tapio91]. The binding targets of MalT consist of 10-nucleotide-long direct repeat sequences that possess conserved motifs; each monomer binds to one of these conserved sequences [Tapio91].

The gene malT is located upstream of the operon malPQ and in the opposite direction [Boos98, Boos00, Schlegel02]. This transcriptional activator [Cole86] belongs to the LuxR family of activators. MalT subunits consist of four domains: the C-terminal DNA-binding domain, the N-terminal ATP-binding domain, and two domains (DT2 and DT3) involved in effector recognition (maltotriose) [Richet05, Danot01, Steegborn01, VidalIngigliard93, Schlegel02a]. Based on an alanine-scanning mutagenesis approach, it was shown that the inducer maltotriose binds inside the cavity of the tetratricopeptide-like sensor domain of MalT, a bacterial STAND transcription factor [Danot10]. Maltotriose plays a dual role in signal transduction by MalT; it triggers nucleotide-binding oligomerization domain (NOD) opening and renders the MalT multimeric platform competent for downstream signaling [Liu13b].

MalT activity is negatively regulated by Aes and MalY through direct protein-protein interactions and competition with maltotriose for MalT binding [Mandrich02, Joly02, Schlegel02a, Schreiber00]. These characteristics point toward identical modes of action for MalY and Aes. However, the identification of an amino acid substitution in MalT that suppresses Aes inhibition without interfering with MalY inhibition suggests that the binding sites of the two inhibitory proteins are not the same [Joly02, Schlegel02a]. In addition, MalK inhibits maltotriose binding by MalT; interestingly, however, MalK interacts directly with MalT in the absence of maltotriose but not in the presence of maltotriose [Joly04, Richet05].

Sequence Length: 901 AAs

Molecular Weight: 103.12 kD (from nucleotide sequence)

In Reactions of unknown directionality:

Not in pathways:
MalT + maltotriose + ATP = MalT-maltotriose-ATP

GO Terms:

Biological Process: GO:2000144 - positive regulation of DNA-templated transcription, initiation Inferred from experiment [Richet87]
Molecular Function: GO:0005524 - ATP binding Inferred from experiment [Richet89]
GO:0044212 - transcription regulatory region DNA binding Inferred from experiment [Danot96]
GO:0048031 - trisaccharide binding Inferred from experiment [Danot10]

MultiFun Terms: information transfer RNA related Transcription related
metabolism carbon utilization carbon compounds
regulation genetic unit regulated operon
regulation type of regulation transcriptional level activator

DNA binding site length: 10 base-pairs

Symmetry: Asymmetric

Consensus DNA Binding Sequence: GGGGAGGAGG

Regulated Transcription Units (5 total): ?

Notes:


Sequence Features

Feature Class Location Citations Comment
Protein-Segment 1 -> 241
[UniProt10]
UniProt: DT1; Sequence Annotation Type: region of interest;
Nucleotide-Phosphate-Binding-Region 39 -> 46
[UniProt10]
UniProt: ATP; Non-Experimental Qualifier: potential;
Sequence-Conflict 192 -> 193
[Cole86, UniProt10a]
Alternate sequence: KQ → NE; UniProt: (in Ref. 1; AAA83888/AAA58216);
Protein-Segment 242 -> 436
[UniProt10]
UniProt: DT2; Sequence Annotation Type: region of interest;
Protein-Segment 437 -> 806
[UniProt10]
UniProt: DT3; Sequence Annotation Type: region of interest;
Conserved-Region 829 -> 894
[UniProt09]
UniProt: HTH luxR-type;
DNA-Binding-Region 853 -> 872
[UniProt10]
UniProt: H-T-H motif; Non-Experimental Qualifier: potential;


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
10/20/97 Gene b3418 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10562; confirmed by SwissProt match.


References

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Boos00: Boos W, Bohm A (2000). "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. PMID: 10973069

Boos98: Boos W, Shuman H (1998). "Maltose/maltodextrin system of Escherichia coli: transport, metabolism, and regulation." Microbiol Mol Biol Rev 62(1);204-29. PMID: 9529892

Butland05: Butland G, Peregrin-Alvarez JM, Li J, Yang W, Yang X, Canadien V, Starostine A, Richards D, Beattie B, Krogan N, Davey M, Parkinson J, Greenblatt J, Emili A (2005). "Interaction network containing conserved and essential protein complexes in Escherichia coli." Nature 433(7025);531-7. PMID: 15690043

Chapon82: Chapon C (1982). "Role of the catabolite activator protein in the maltose regulon of Escherichia coli." J Bacteriol 150(2);722-9. PMID: 7040340

Chapon83: Chapon C, Kolb A (1983). "Action of CAP on the malT promoter in vitro." J Bacteriol 156(3);1135-43. PMID: 6315676

Cole86: Cole ST, Raibaud O (1986). "The nucleotide sequence of the malT gene encoding the positive regulator of the Escherichia coli maltose regulon." Gene 1986;42(2);201-8. PMID: 3015733

Danot01: Danot O (2001). "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. PMID: 11209048

Danot10: Danot O (2010). "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. PMID: 20545845

Danot94: Danot O, Raibaud O (1994). "Multiple protein-DNA and protein-protein interactions are involved in transcriptional activation by MalT." Mol Microbiol 1994;14(2);335-46. PMID: 7830577

Danot96: Danot O, Vidal-Ingigliardi D, Raibaud O (1996). "Two amino acid residues from the DNA-binding domain of MalT play a crucial role in transcriptional activation." J Mol Biol 262(1);1-11. PMID: 8809174

Dethiollaz96: Dethiollaz S, Eichenberger P, Geiselmann J (1996). "Influence of DNA geometry on transcriptional activation in Escherichia coli." EMBO J 15(19);5449-58. PMID: 8895588

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Eichenberger96: Eichenberger P, Dethiollaz S, Fujita N, Ishihama A, Geiselmann J (1996). "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. PMID: 8952481

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Joly02: Joly N, Danot O, Schlegel A, Boos W, Richet E (2002). "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. PMID: 11867639

Joly04: Joly N, Bohm A, Boos W, Richet E (2004). "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. PMID: 15180985

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Kornacker89: Kornacker MG, Boyd A, Pugsley AP, Plastow GS (1989). "A new regulatory locus of the maltose regulon in Klebsiella pneumoniae strain K21 identified by the study of pullulanase secretion mutants." J Gen Microbiol 1989;135 ( Pt 2);397-408. PMID: 2693596

Liu13b: Liu P, Danot O, Richet E (2013). "A dual role for the inducer in signalling by MalT, a signal transduction ATPase with numerous domains (STAND)." Mol Microbiol 90(6);1309-23. PMID: 24134781

Mandrich02: Mandrich L, Caputo E, Martin BM, Rossi M, Manco G (2002). "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. PMID: 12374803

Marquenet10: Marquenet E, Richet E (2010). "Conserved motifs involved in ATP hydrolysis by MalT, a signal transduction ATPase with numerous domains from Escherichia coli." J Bacteriol 192(19);5181-91. PMID: 20693326

Raibaud89: Raibaud O (1989). "Nucleoprotein structures at positively regulated bacterial promoters: homology with replication origins and some hypotheses on the quaternary structure of the activator proteins in these complexes." Mol Microbiol 1989;3(3);455-8. PMID: 2664421

Raibaud89a: Raibaud O, Vidal-Ingigliardi D, Richet E (1989). "A complex nucleoprotein structure involved in activation of transcription of two divergent Escherichia coli promoters." J Mol Biol 1989;205(3);471-85. PMID: 2538630

Rajagopala14: Rajagopala SV, Sikorski P, Kumar A, Mosca R, Vlasblom J, Arnold R, Franca-Koh J, Pakala SB, Phanse S, Ceol A, Hauser R, Siszler G, Wuchty S, Emili A, Babu M, Aloy P, Pieper R, Uetz P (2014). "The binary protein-protein interaction landscape of Escherichia coli." Nat Biotechnol 32(3);285-90. PMID: 24561554

Richet05: Richet E, Joly N, Danot O (2005). "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. PMID: 15733913

Richet87: Richet E, Raibaud O (1987). "Purification and properties of the MalT protein, the transcription activator of the Escherichia coli maltose regulon." J Biol Chem 262(26);12647-53. PMID: 3305511

Richet89: Richet E, Raibaud O (1989). "MalT, the regulatory protein of the Escherichia coli maltose system, is an ATP-dependent transcriptional activator." EMBO J 1989;8(3);981-7. PMID: 2524384

Ritzefeld11: Ritzefeld M, Wollschlager K, Niemann G, Anselmetti D, Sewald N (2011). "Minor groove recognition is important for the transcription factor PhoB: a surface plasmon resonance study." Mol Biosyst 7(11);3132-42. PMID: 21912786

Schlegel02: Schlegel A, Bohm A, Lee SJ, Peist R, Decker K, Boos W (2002). "Network regulation of the Escherichia coli maltose system." J Mol Microbiol Biotechnol 4(3);301-7. PMID: 11931562

Schlegel02a: Schlegel A, Danot O, Richet E, Ferenci T, Boos W (2002). "The N terminus of the Escherichia coli transcription activator MalT is the domain of interaction with MalY." J Bacteriol 184(11);3069-77. PMID: 12003949

Schneider92: Schneider E, Freundlieb S, Tapio S, Boos W (1992). "Molecular characterization of the MalT-dependent periplasmic alpha-amylase of Escherichia coli encoded by malS." J Biol Chem 1992;267(8);5148-54. PMID: 1544897

Schreiber00: Schreiber V, Steegborn C, Clausen T, Boos W, Richet E (2000). "A new mechanism for the control of a prokaryotic transcriptional regulator: antagonistic binding of positive and negative effectors." Mol Microbiol 35(4);765-76. PMID: 10692154

Steegborn01: Steegborn C, Danot O, Huber R, Clausen T (2001). "Crystal structure of transcription factor MalT domain III: a novel helix repeat fold implicated in regulated oligomerization." Structure 9(11);1051-60. PMID: 11709169

Tapio91: Tapio S, Yeh F, Shuman HA, Boos W (1991). "The malZ gene of Escherichia coli, a member of the maltose regulon, encodes a maltodextrin glucosidase." J Biol Chem 1991;266(29);19450-8. PMID: 1918057

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

UniProt10: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

VidalIngigliard93: Vidal-Ingigliardi D, Richet E, Danot O, Raibaud O (1993). "A small C-terminal region of the Escherichia coli MalT protein contains the DNA-binding domain." J Biol Chem 268(33);24527-30. PMID: 8227007

Other References Related to Gene Regulation

Chapon82a: Chapon C (1982). "Expression of malT, the regulator gene of the maltose region in Escherichia coli, is limited both at transcription and translation." EMBO J 1(3);369-74. PMID: 6325162

Decker98: Decker K, Plumbridge J, Boos W (1998). "Negative transcriptional regulation of a positive regulator: the expression of malT, encoding the transcriptional activator of the maltose regulon of Escherichia coli, is negatively controlled by Mlc." Mol Microbiol 1998;27(2);381-90. PMID: 9484893

Eichenberger97: Eichenberger P, Dethiollaz S, Buc H, Geiselmann J (1997). "Structural kinetics of transcription activation at the malT promoter of Escherichia coli by UV laser footprinting." Proc Natl Acad Sci U S A 94(17);9022-7. PMID: 9256428

Johansson98: Johansson J, Dagberg B, Richet E, Uhlin BE (1998). "H-NS and StpA proteins stimulate expression of the maltose regulon in Escherichia coli." J Bacteriol 180(23);6117-25. PMID: 9829919

Menendez87: Menendez M, Kolb A, Buc H (1987). "A new target for CRP action at the malT promoter." EMBO J 1987;6(13);4227-34. PMID: 2832158

Park10a: Park HS, Ostberg Y, Johansson J, Wagner EG, Uhlin BE (2010). "Novel role for a bacterial nucleoid protein in translation of mRNAs with suboptimal ribosome-binding sites." Genes Dev 24(13);1345-50. PMID: 20595230

Plumbridge01: Plumbridge J (2001). "DNA binding sites for the Mlc and NagC proteins: regulation of nagE, encoding the N-acetylglucosamine-specific transporter in Escherichia coli." Nucleic Acids Res 29(2);506-14. PMID: 11139621

Tchetina95: Tchetina E, Newman EB (1995). "Identification of Lrp-regulated genes by inverse PCR and sequencing: regulation of two mal operons of Escherichia coli by leucine-responsive regulatory protein." J Bacteriol 1995;177(10);2679-83. PMID: 7751276


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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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