Escherichia coli K-12 substr. MG1655 Polypeptide: maltose ABC transporter - membrane subunit

Gene: malG Accession Numbers: EG10556 (EcoCyc), b4032, ECK4024

Regulation Summary Diagram: ?

Regulation summary diagram for malG

Component of: maltose ABC transporter (extended summary available)

MalG is an integral membrane component of the maltose ABC transporter.

Gene Citations: [Francoz88]

Locations: inner membrane

Map Position: [4,240,649 <- 4,241,539] (91.4 centisomes, 329°)
Length: 891 bp / 296 aa

Molecular Weight of Polypeptide: 32.225 kD (from nucleotide sequence), 22.0 kD (experimental) [Dassa85 ]

Unification Links: ASAP:ABE-0013193 , CGSC:530 , DIP:DIP-59709N , EchoBASE:EB0551 , EcoGene:EG10556 , EcoliWiki:b4032 , OU-Microarray:b4032 , PortEco:malG , PR:PRO_000023149 , Pride:P68183 , Protein Model Portal:P68183 , RefSeq:NP_418456 , RegulonDB:EG10556 , SMR:P68183 , String:511145.b4032 , UniProt:P68183

Relationship Links: InterPro:IN-FAMILY:IPR000515 , PDB:Structure:2r6g , PDB:Structure:3FH6 , PDB:Structure:3PUV , PDB:Structure:3PUW , PDB:Structure:3PUX , PDB:Structure:3PUY , PDB:Structure:3PUZ , PDB:Structure:3PV0 , PDB:Structure:3RLF , PDB:Structure:4JBW , Pfam:IN-FAMILY:PF00528 , Prosite:IN-FAMILY:PS50928

In Paralogous Gene Group: 24 (43 members)

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Genetic Regulation Schematic: ?

Genetic regulation schematic for malG

GO Terms:

Biological Process: GO:0015768 - maltose transport Inferred from experiment [Davidson91]
GO:0042956 - maltodextrin transport Inferred from experiment [Ferenci80]
GO:0006810 - transport Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0008643 - carbohydrate transport Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0015423 - maltose-transporting ATPase activity Inferred from experiment [Davidson91]
GO:0015609 - maltooligosaccharide-importing ATPase activity Inferred from experiment [Ferenci80]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, DiazMejia09, Daley05, Dassa90a]
GO:0016020 - membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA01a, Wagner08]
GO:0043190 - ATP-binding cassette (ABC) transporter complex Inferred from experiment [Davidson91]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell structure membrane
metabolism carbon utilization carbon compounds
transport Channel-type Transporters Pyrophosphate Bond (ATP; GTP; P2) Hydrolysis-driven Active Transporters The ATP-binding Cassette (ABC) Superfamily + ABC-type Uptake Permeases ABC superfamily, membrane component

Essentiality data for malG knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 1]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 2]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 1]
Yes [Feist07, Comment 3]

Subunit of: maltose ABC transporter

Subunit composition of maltose ABC transporter = [MalK]2[MalF][MalG][MalE]
         maltose ABC transporter - ATP binding subunit = MalK (summary available)
         maltose ABC transporter - membrane subunit = MalF (summary available)
         maltose ABC transporter - membrane subunit = MalG (summary available)
         maltose ABC transporter - periplasmic binding protein = MalE (extended summary available)

MalKFGE is a maltose transport system that is a member of the ATP-Binding Cassette (ABC) Superfamily of transporters [Wu95]. MalE is the periplasmic maltose-binding protein, MalF and MalG are the integral membrane components, and MalK is the ATP-binding component of the ABC transporter, peripherally associated with the inner membrane through its interactions with MalF and MalG. The maltose ABC transporter is capable of transporting malto-oligosaccharides up to seven glucose units long [Ferenci80]. The maltose transporter also functions to regulate gene expression through direct interaction with its cognate transcriptional regulator MalT [Richet12].

The crystal structure of the maltose ABC transporter has been determined in 3 differing conformations: an inward facing 'resting' state with the maltose binding pocket only accessible from the cytoplasm and the nucleotide binding interface in an open conformation [Khare09]; an outward facing conformation with the substrate binding pocket open towards the periplasmic space and ATP bound at the cytoplasmic nucleotide binding interface [Oldham07] and an intermediate 'pre-translocation' structure with an occluded maltose binding pocket and no ATP bound [Oldham11].

The structure of MalE has been studied extensively [Sharff92, Spurlino91, Sharff95, Sharff93, Shilton96, Quiocho97, Mueller00, Duan01, Duan02, Rubin02a, Srinivasan02, Saul03, Telmer03, Binz04, Telmer05, Kainosho06, Xu06d, Tang07]. The crystal structure of the dimeric MalK has also been determined with bound ADP to a resolution of 2.3 Å [Lu05a], with ATP bound to 2.60 Å, in a nucleotide-free, open state to 2.8 Å, and in a nucleotide-free semi-open state to 2.9 Å [Chen03b]. The N-terminal portion of MalK is the ATP-binding portion which interacts with MalF and MalG, and the C-terminal portion is a regulatory domain that interacts with MalT to prevent transcription of mal genes [Higgins85, Bohm02, Samanta03, Chen03b]. Binding of ATP to MalK is required for stabilization of the MalEFGK2 complex [Chen01]. Binding of ATP to MalK results in closure of the MalK dimer interface and transmission of a signal through MalF and MalG causing the opening of MalE to release maltose into the transporter [Mourez98, Mannering01, Austermuhle04, Daus06, Oloo06, Wen08]. Binding of MalE to the MalF and MalG subunits of MalFGK2 stimulates ATPase activity of the MalK subunits coupled to substrate transport [Chen01, Daus07]. The signal for stimulation of ATPase activity is transduced through MalF and MalG [Davidson92, Covitz94]. The interaction of MalF,and in particular the large periplasmic loop of MalF, with MalE has been studied [Daus09, Jacso09].

A 10-fold increase in the level of maltose transport activity was observed in membrane vesicles when the membrane associated components of the transport system (MalF, MalG, and MalK) were overproduced [Davidson90]. Maltose transport activity was abolished in proteoliposomes prepared from a strain with a deletion of the mal genes [Davidson90]. The purified MalKFGE complex exhibits transport-associated ATPase activity, and mutations in the malK gene resulted in loss of ATPase and transport activities without affecting protein stability [Davidson91, Panagiotidis93, Davidson97]. malF mutants are able to transport lactose through the maltose ABC transporter [Merino97, Merino98].

Expression of the malE and malK operons is activated by MalT and cAMP-CRP [VidalIngigliard91, Chapon82, Hofnung74, Hofnung74a]. Inactive (ATP-bound) MalK inhibits the activation of MalT by competing with the binding of the inducer, maltotriose, to MalT [Joly04, Reyes88]. MalK with hydrolysed ATP no longer associates with and inhibits MalT [Panagiotidis98]. Inhibition involves sequestration of MalT by the resting form of the MalFGK transporter, not by free MalK. In the absence of maltose, MalT is sequestered by the maltose transporter via a MalK-MalT interaction; upon addition of maltose to the culture medium, MalT is released from the membrane [Richet12]. This mechanism prevents the induction of malT by endogenously produced maltotriose and directly couples transport with the activation of a transcriptional regulator.

MalY and Aes also inhibit activation of MalT by competing with maltotriose [Reidl91, Schreiber00, Clausen00, Joly02, Schlegel02a]. Lrp activates expression of the malE and malK operons [Tchetina95]. Mlc acts as a repressor of malT expression [Decker98]. Transcription of malE is regulated by the CreBC two-component system [Avison01]. MalK activity is also subject to inducer exclusion, that is, direct allosteric inhibition, by the dephosphorylated form of EIIAGlc. Addition of EIIAGlc inhibits the activity of the maltose transporter reconstituted in proteopliposomes [Dean90, Bao13]. The pH-dependent transcription of the maltose regulon is dependent upon the level of cAMP-CRP [Chagneau01, Alonzo98].

Targeting of MalE to the Sec-translocase for transport across the inner membrane is SecB-dependent [Bechtluft07, Baars06]. Insertion of MalF into the cytoplasmic membrane is SecE- and SecA-dependent [Traxler96, Saaf95], though evidence to the contrary has been presented [McGovern91].

Reviews: [Schlegel02, Boos98, Nikaido94, Shuman93, Bordignon10, Gorke12, Chen13a].

Citations: [Daus07a, Sharma05, Richet05, Kennedy04, Steinke01, Sharma00b, Hunke00, ReichSlotky00, Decker99, Kennedy99, Nelson98, Panagiotidis98a, Hall98a, Mourez97, Mourez97a, Dassa97, Lippincott97, Meyer97, Richet96, Zhang96a, Ehrle96, Schneider95, Hekstra93, Boyd93, Dassa93, Dassa93a, Traxler92, Dean92, McGovern91a, Ehrmann91, Ehrmann90, Wyka90, Francoz88, Froshauer88, Newbury87, Boyd87, Ehrmann87, Duplay87, Bukau86, Froshauer84, Kiino84, Bedouelle83, Ohsumi83, Gilson82, Bedouelle82, Ohki82, Shuman82, Bedouelle82a, Shuman81, Colonna81, Wandersman79, Raibaud79, Silhavy79, Raibaud79a, Randall78, Bao13a]

Locations: inner membrane

Relationship Links: PDB:Structure:2R6G , PDB:Structure:3FH6 , PDB:Structure:3PUY , PDB:Structure:3PUZ , PDB:Structure:3PV0

GO Terms:

Biological Process: GO:0015768 - maltose transport Inferred from experiment [Davidson91]
Molecular Function: GO:0015423 - maltose-transporting ATPase activity Inferred from experiment [Davidson91]
GO:0015609 - maltooligosaccharide-importing ATPase activity Inferred from experiment [Ferenci80]
GO:0033613 - activating transcription factor binding Inferred from experiment [Richet12]
Cellular Component: GO:0043190 - ATP-binding cassette (ABC) transporter complex Inferred from experiment [Davidson91]

Enzymatic reaction of: maltotetraose ABC transporter (maltose ABC transporter)

EC Number: 3.6.3.-

Transport reaction diagram for maltotetraose ABC transporter

Enzymatic reaction of: maltotriose ABC transporter (maltose ABC transporter)

EC Number: 3.6.3.-

Transport reaction diagram for maltotriose ABC transporter

Enzymatic reaction of: maltose ABC transporter

Synonyms: Transport of maltose

EC Number:

Transport reaction diagram for maltose ABC transporter

Alternative Products for maltose: maltohexaose [Ferenci80 ] , maltopentaose [Ferenci80 ] , maltoheptaose [Ferenci80 ]

Sequence Features

Protein sequence of maltose ABC transporter - membrane subunit with features indicated

Feature Class Location Common Name Citations Comment
Transmembrane-Region 18 -> 37 MalG TM1
Transmembrane-Region 19 -> 39  
UniProt: Helical;; Non-Experimental Qualifier: probable;
Transmembrane-Region 81 -> 102 MalG TM2
Transmembrane-Region 82 -> 102  
UniProt: Helical;; Non-Experimental Qualifier: probable;
Conserved-Region 85 -> 281  
UniProt: ABC transmembrane type-1;
Transmembrane-Region 123 -> 150 MalG TM3
Transmembrane-Region 124 -> 144  
UniProt: Helical;; Non-Experimental Qualifier: probable;
Transmembrane-Region 151 -> 171  
UniProt: Helical;; Non-Experimental Qualifier: probable;
Transmembrane-Region 161 -> 175 MalG TM4
Mutagenesis-Variant 190  
[Hunke00, Mourez97a, UniProt11]
E → A, C, K or L: Reduction of transport rate.
Mutagenesis-Variant 192  
[Hunke00, Mourez97a, UniProt11]
A → D, L or S: Loss of transport and malK dissociation from the membrane.
Mutagenesis-Variant 196  
[Hunke00, Mourez97a, UniProt11]
[Hunke00, Mourez97a, UniProt11]
G → P: Loss of transport and malK dissociation from the membrane.
G → A: No effect.
Transmembrane-Region 205 -> 225  
UniProt: Helical;; Non-Experimental Qualifier: probable;
Mutagenesis-Variant 209  
[Mourez97a, UniProt11]
UniProt: No effect.
Transmembrane-Region 217 -> 236 MalG TM5
Transmembrane-Region 260 -> 280  
UniProt: Helical;; Non-Experimental Qualifier: probable;
Transmembrane-Region 263 -> 279 MalG TM6

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Units:

Transcription-unit diagram

Transcription-unit diagram


10/20/97 Gene b4032 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10556; confirmed by SwissProt match.


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Bao13: Bao H, Duong F (2013). "Phosphatidylglycerol directs binding and inhibitory action of EIIAGlc protein on the maltose transporter." J Biol Chem 288(33);23666-74. PMID: 23821551

Bao13a: Bao H, Duong F (2013). "ATP alone triggers the outward facing conformation of the maltose ATP-binding cassette transporter." J Biol Chem 288(5);3439-48. PMID: 23243313

Bechtluft07: Bechtluft P, van Leeuwen RG, Tyreman M, Tomkiewicz D, Nouwen N, Tepper HL, Driessen AJ, Tans SJ (2007). "Direct observation of chaperone-induced changes in a protein folding pathway." Science 318(5855);1458-61. PMID: 18048690

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Bohm02: Bohm A, Diez J, Diederichs K, Welte W, Boos W (2002). "Structural model of MalK, the ABC subunit of the maltose transporter of Escherichia coli: implications for mal gene regulation, inducer exclusion, and subunit assembly." J Biol Chem 277(5);3708-17. PMID: 11709552

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

Bordignon10: Bordignon E, Grote M, Schneider E (2010). "The maltose ATP-binding cassette transporter in the 21st century--towards a structural dynamic perspective on its mode of action." Mol Microbiol 77(6);1354-66. PMID: 20659291

Boyd87: Boyd D, Manoil C, Beckwith J (1987). "Determinants of membrane protein topology." Proc Natl Acad Sci U S A 84(23);8525-9. PMID: 3317413

Boyd93: Boyd D, Traxler B, Beckwith J (1993). "Analysis of the topology of a membrane protein by using a minimum number of alkaline phosphatase fusions." J Bacteriol 175(2);553-6. PMID: 8419303

Bukau86: Bukau B, Ehrmann M, Boos W (1986). "Osmoregulation of the maltose regulon in Escherichia coli." J Bacteriol 166(3);884-91. PMID: 2423504

Chagneau01: Chagneau C, Heyde M, Alonso S, Portalier R, Laloi P (2001). "External-pH-dependent expression of the maltose regulon and ompF gene in Escherichia coli is affected by the level of glycerol kinase, encoded by glpK." J Bacteriol 183(19);5675-83. PMID: 11544231

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

Chen01: Chen J, Sharma S, Quiocho FA, Davidson AL (2001). "Trapping the transition state of an ATP-binding cassette transporter: evidence for a concerted mechanism of maltose transport." Proc Natl Acad Sci U S A 98(4);1525-30. PMID: 11171984

Chen03b: Chen J, Lu G, Lin J, Davidson AL, Quiocho FA (2003). "A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle." Mol Cell 12(3);651-61. PMID: 14527411

Chen13a: Chen J (2013). "Molecular mechanism of the Escherichia coli maltose transporter." Curr Opin Struct Biol. PMID: 23628288

Clausen00: Clausen T, Schlegel A, Peist R, Schneider E, Steegborn C, Chang YS, Haase A, Bourenkov GP, Bartunik HD, Boos W (2000). "X-ray structure of MalY from Escherichia coli: a pyridoxal 5'-phosphate-dependent enzyme acting as a modulator in mal gene expression." EMBO J 19(5);831-42. PMID: 10698925

Colonna81: Colonna B, Hofnung M (1981). "rho Mutations restore lamB expression in E. coli K12 strains with an inactive malB region." Mol Gen Genet 184(3);479-83. PMID: 6278260

Covitz94: Covitz KM, Panagiotidis CH, Hor LI, Reyes M, Treptow NA, Shuman HA (1994). "Mutations that alter the transmembrane signalling pathway in an ATP binding cassette (ABC) transporter." EMBO J 13(7);1752-9. PMID: 8157012

Daley05: Daley DO, Rapp M, Granseth E, Melen K, Drew D, von Heijne G (2005). "Global topology analysis of the Escherichia coli inner membrane proteome." Science 308(5726);1321-3. PMID: 15919996

Dassa85: Dassa E, Hofnung M (1985). "Sequence of gene malG in E. coli K12: homologies between integral membrane components from binding protein-dependent transport systems." EMBO J 4(9);2287-93. PMID: 3000770

Dassa90a: Dassa E (1990). "Cellular localization of the MalG protein from the maltose transport system in Escherichia coli K12." Mol Gen Genet 222(1);33-6. PMID: 2233678

Dassa93: Dassa E (1993). "Sequence-function relationships in MalG, an inner membrane protein from the maltose transport system in Escherichia coli." Mol Microbiol 7(1);39-47. PMID: 8437519

Dassa93a: Dassa E, Muir S (1993). "Membrane topology of MalG, an inner membrane protein from the maltose transport system of Escherichia coli." Mol Microbiol 7(1);29-38. PMID: 8437518

Dassa97: Dassa E, Lambert P (1997). "Activity of protein MalE (maltose-binding protein) fused to cytoplasmic and periplasmic regions of an Escherichia coli inner membrane protein." Res Microbiol 148(5);389-95. PMID: 9765817

Daus06: Daus ML, Landmesser H, Schlosser A, Muller P, Herrmann A, Schneider E (2006). "ATP induces conformational changes of periplasmic loop regions of the maltose ATP-binding cassette transporter." J Biol Chem 281(7);3856-65. PMID: 16352608

Daus07: Daus ML, Berendt S, Wuttge S, Schneider E (2007). "Maltose binding protein (MalE) interacts with periplasmic loops P2 and P1 respectively of the MalFG subunits of the maltose ATP binding cassette transporter (MalFGK(2)) from Escherichia coli/Salmonella during the transport cycle." Mol Microbiol 66(5);1107-22. PMID: 17961142

Daus07a: Daus ML, Grote M, Muller P, Doebber M, Herrmann A, Steinhoff HJ, Dassa E, Schneider E (2007). "ATP-driven MalK dimer closure and reopening and conformational changes of the "EAA" motifs are crucial for function of the maltose ATP-binding cassette transporter (MalFGK2)." J Biol Chem 282(31);22387-96. PMID: 17545154

Daus09: Daus ML, Grote M, Schneider E (2009). "The MalF P2 loop of the ATP-binding cassette transporter MalFGK2 from Escherichia coli and Salmonella enterica serovar typhimurium interacts with maltose binding protein (MalE) throughout the catalytic cycle." J Bacteriol 191(3);754-61. PMID: 19047355

Davidson90: Davidson AL, Nikaido H (1990). "Overproduction, solubilization, and reconstitution of the maltose transport system from Escherichia coli." J Biol Chem 1990;265(8);4254-60. PMID: 2155217

Davidson91: Davidson AL, Nikaido H (1991). "Purification and characterization of the membrane-associated components of the maltose transport system from Escherichia coli." J Biol Chem 266(14);8946-51. PMID: 2026607

Davidson92: Davidson AL, Shuman HA, Nikaido H (1992). "Mechanism of maltose transport in Escherichia coli: transmembrane signaling by periplasmic binding proteins." Proc Natl Acad Sci U S A 89(6);2360-4. PMID: 1549599

Davidson97: Davidson AL, Sharma S (1997). "Mutation of a single MalK subunit severely impairs maltose transport activity in Escherichia coli." J Bacteriol 179(17);5458-64. PMID: 9287001

Dean90: Dean DA, Reizer J, Nikaido H, Saier MH (1990). "Regulation of the maltose transport system of Escherichia coli by the glucose-specific enzyme III of the phosphoenolpyruvate-sugar phosphotransferase system. Characterization of inducer exclusion-resistant mutants and reconstitution of inducer exclusion in proteoliposomes." J Biol Chem 265(34);21005-10. PMID: 2250006

Dean92: Dean DA, Hor LI, Shuman HA, Nikaido H (1992). "Interaction between maltose-binding protein and the membrane-associated maltose transporter complex in Escherichia coli." Mol Microbiol 6(15);2033-40. PMID: 1406246

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

Decker99: Decker K, Gerhardt F, Boos W (1999). "The role of the trehalose system in regulating the maltose regulon of Escherichia coli." Mol Microbiol 32(4);777-88. PMID: 10361281

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

Duan01: Duan X, Hall JA, Nikaido H, Quiocho FA (2001). "Crystal structures of the maltodextrin/maltose-binding protein complexed with reduced oligosaccharides: flexibility of tertiary structure and ligand binding." J Mol Biol 306(5);1115-26. PMID: 11237621

Duan02: Duan X, Quiocho FA (2002). "Structural evidence for a dominant role of nonpolar interactions in the binding of a transport/chemosensory receptor to its highly polar ligands." Biochemistry 41(3);706-12. PMID: 11790091

Duplay87: Duplay P, Szmelcman S, Bedouelle H, Hofnung M (1987). "Silent and functional changes in the periplasmic maltose-binding protein of Escherichia coli K12. I. Transport of maltose." J Mol Biol 194(4);663-73. PMID: 2821264

Ehrle96: Ehrle R, Pick C, Ulrich R, Hofmann E, Ehrmann M (1996). "Characterization of transmembrane domains 6, 7, and 8 of MalF by mutational analysis." J Bacteriol 178(8);2255-62. PMID: 8636026

Ehrmann87: Ehrmann M, Boos W (1987). "Identification of endogenous inducers of the mal regulon in Escherichia coli." J Bacteriol 1987;169(8);3539-45. PMID: 3038842

Ehrmann90: Ehrmann M, Boyd D, Beckwith J (1990). "Genetic analysis of membrane protein topology by a sandwich gene fusion approach." Proc Natl Acad Sci U S A 87(19);7574-8. PMID: 2170984

Ehrmann91: Ehrmann M, Beckwith J (1991). "Proper insertion of a complex membrane protein in the absence of its amino-terminal export signal." J Biol Chem 266(25);16530-3. PMID: 1885584

Feist07: Feist AM, Henry CS, Reed JL, Krummenacker M, Joyce AR, Karp PD, Broadbelt LJ, Hatzimanikatis V, Palsson BO (2007). "A genome-scale metabolic reconstruction for Escherichia coli K-12 MG1655 that accounts for 1260 ORFs and thermodynamic information." Mol Syst Biol 3;121. PMID: 17593909

Ferenci80: Ferenci T (1980). "The recognition of maltodextrins by Escherichia coli." Eur J Biochem 108(2);631-6. PMID: 6997044

Francoz88: Francoz E, Dassa E (1988). "3' end of the malEFG operon in E.coli: localization of the transcription termination site." Nucleic Acids Res 1988;16(9);4097-109. PMID: 2836810

Froshauer84: Froshauer S, Beckwith J (1984). "The nucleotide sequence of the gene for malF protein, an inner membrane component of the maltose transport system of Escherichia coli. Repeated DNA sequences are found in the malE-malF intercistronic region." J Biol Chem 259(17);10896-903. PMID: 6088520

Froshauer88: Froshauer S, Green GN, Boyd D, McGovern K, Beckwith J (1988). "Genetic analysis of the membrane insertion and topology of MalF, a cytoplasmic membrane protein of Escherichia coli." J Mol Biol 200(3);501-11. PMID: 3294421

Gilson82: Gilson E, Nikaido H, Hofnung M (1982). "Sequence of the malK gene in E.coli K12." Nucleic Acids Res 10(22);7449-58. PMID: 6296778

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

Gorke12: Gorke B (2012). "Killing two birds with one stone: an ABC transporter regulates gene expression through sequestration of a transcriptional regulator at the membrane." Mol Microbiol 85(4);597-601. PMID: 22742494

Hall98a: Hall JA, Davidson AL, Nikaido H (1998). "Preparation and reconstitution of membrane-associated maltose transporter complex of Escherichia coli." Methods Enzymol 292;20-9. PMID: 9711543

Hekstra93: Hekstra D, Tommassen J (1993). "Functional exchangeability of the ABC proteins of the periplasmic binding protein-dependent transport systems Ugp and Mal of Escherichia coli." J Bacteriol 1993;175(20);6546-52. PMID: 8407831

Higgins85: Higgins CF, Hiles ID, Whalley K, Jamieson DJ (1985). "Nucleotide binding by membrane components of bacterial periplasmic binding protein-dependent transport systems." EMBO J 4(4);1033-9. PMID: 3926486

Hofnung74: Hofnung M (1974). "Divergent operons and the genetic structure of the maltose B region in Escherichia coli K12." Genetics 76(2);169-84. PMID: 4595640

Hofnung74a: Hofnung M, Hatfield D, Schwartz M (1974). "malB region in Escherichia coli K-12: characterization of new mutations." J Bacteriol 117(1);40-7. PMID: 4587612

Hunke00: Hunke S, Mourez M, Jehanno M, Dassa E, Schneider E (2000). "ATP modulates subunit-subunit interactions in an ATP-binding cassette transporter (MalFGK2) determined by site-directed chemical cross-linking." J Biol Chem 275(20);15526-34. PMID: 10809785

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Other References Related to Gene Regulation

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Merkel92: Merkel TJ, Nelson DM, Brauer CL, Kadner RJ (1992). "Promoter elements required for positive control of transcription of the Escherichia coli uhpT gene." J Bacteriol 1992;174(9);2763-70. PMID: 1569008

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Richet00: Richet E (2000). "Synergistic transcription activation: a dual role for CRP in the activation of an Escherichia coli promoter depending on MalT and CRP." EMBO J 19(19);5222-32. PMID: 11013224

Richet91: Richet E, Raibaud O (1991). "Supercoiling is essential for the formation and stability of the initiation complex at the divergent malEp and malKp promoters." J Mol Biol 218(3);529-42. PMID: 2016744

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