RegulonDB

Gene
Name:	malE
Synonym(s):	ECK4026, EG10554, b4034
Genome position(nucleotides):	4245229 <-- 4246419
Strand:	reverse
Sequence:	Get nucleotide sequence FastaFormat
GC content %:	51.05
External database links:

ASAP:	ABE-0013200
CGSC:	532
ECHOBASE:	EB0549
ECOLIHUB:	malE
OU-MICROARRAY:	b4034
STRING:	511145.b4034
COLOMBOS:	malE

Product

Name:

maltose ABC transporter periplasmic binding protein

Synonym(s):

MBP, MalE, maltodextrin binding protein, maltose binding protein

Sequence:

Get amino acid sequence Fasta Format

Cellular location:

inner membrane,periplasmic space

Molecular weight:

43.388

Isoelectric point:

5.359

Motif(s):

Type	Positions	Sequence	Comment
	1 -> 26	MKIKTGARILALSALTTMMFSASALA
	27 -> 396	KIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTRITK	UniProt: Maltose/maltodextrin-binding periplasmic protein.
	36 -> 36	W	UniProt: In Ref. 8; AA sequence..
	45 -> 315	GLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEG
	46 -> 46	L	UniProt: In Ref. 5; CAA23581..

Classification:

Multifun Terms (GenProtEC)
		5 - cell processes --> 5.3 - motility, chemotaxis, energytaxis (aerotaxis, redoxtaxis etc)
		4 - transport --> 4.3 - Primary Active Transporters --> 4.3.A - Pyrophosphate Bond (ATP; GTP; P2) Hydrolysis-driven Active Transporters --> 4.3.A.1 - The ATP-binding Cassette (ABC) Superfamily + ABC-type Uptake Permeases --> 4.3.A.1.p - ABC superfamily, periplasmic binding component
Gene Ontology Terms (GO)
	cellular_component	GO:0016020 - membrane GO:0030288 - outer membrane-bounded periplasmic space GO:0042597 - periplasmic space GO:0043190 - ATP-binding cassette (ABC) transporter complex GO:0055052 - ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing GO:1990060 - maltose transport complex
	molecular_function	GO:0005515 - protein binding GO:0015144 - carbohydrate transmembrane transporter activity GO:1901982 - maltose binding
	biological_process	GO:0006974 - cellular response to DNA damage stimulus GO:0008643 - carbohydrate transport GO:0015768 - maltose transport GO:0042956 - maltodextrin transport GO:0055085 - transmembrane transport GO:0034219 - carbohydrate transmembrane transport GO:0034289 - detection of maltose stimulus GO:0060326 - cell chemotaxis

Note(s):

Note(s): ...[more].

Reference(s):

[1] Austermuhle MI., et al., 2004
[2] Bao H., et al., 2012
[3] Binz HK., et al., 2004
[4] Bucher D., et al., 2011
[5] Caldelari I., et al., 2008
[6] Dassa E., et al., 1997
[7] Dean DA., et al., 1992
[8] Ferenci T., et al., 1986
[9] Gardina PJ., et al., 1997
[10] Gould AD., et al., 2009
[11] Hall JA., et al., 1997
[12] Hall JA., et al., 1997
[13] Hall JA., et al., 1997
[14] Hor LI., et al., 1993
[15] Kainosho M., et al., 2006
[16] Kossmann M., et al., 1988
[17] Mascarenhas NM., et al., 2013
[18] Miklos AC., et al., 2013
[19] Quiocho FA., et al., 1979
[20] Sharff AJ., et al., 1993
[21] Tang C., et al., 2007
[22] Telmer PG., et al., 2005
[23] Treptow NA., et al., 1988
[24] Treptow NA., et al., 1985
[25] Walters BT., et al., 2013
[26] Xu Y., et al., 2006
[27] Ye X., et al., 2018
[28] Zhang Y., et al., 1996
[29] van den Noort M., et al., 2021

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UNIPROT:

Transcriptional Regulation
	Display Regulation
Activated by:	CRP, H-NS, MalT, StpA, Fis
Repressed by:	CreB

Reference(s)
[1] Austermuhle MI., Hall JA., Klug CS., Davidson AL., 2004, Maltose-binding protein is open in the catalytic transition state for ATP hydrolysis during maltose transport., J Biol Chem 279(27):28243-50
[2] Bao H., Duong F., 2012, Discovery of an auto-regulation mechanism for the maltose ABC transporter MalFGK2., PLoS One 7(4):e34836
[3] Binz HK., Amstutz P., Kohl A., Stumpp MT., Briand C., Forrer P., Grutter MG., Pluckthun A., 2004, High-affinity binders selected from designed ankyrin repeat protein libraries., Nat Biotechnol 22(5):575-82
[4] Bucher D., Grant BJ., Markwick PR., McCammon JA., 2011, Accessing a hidden conformation of the maltose binding protein using accelerated molecular dynamics., PLoS Comput Biol 7(4):e1002034
[5] Caldelari I., Palmer T., Sargent F., 2008, Escherichia coli tat mutant strains are able to transport maltose in the absence of an active malE gene., Arch Microbiol 189(6):597-604
[6] 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
[7] 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
[8] Ferenci T., Muir M., Lee KS., Maris D., 1986, Substrate specificity of the Escherichia coli maltodextrin transport system and its component proteins., Biochim Biophys Acta 860(1):44-50
[9] Gardina PJ., Bormans AF., Hawkins MA., Meeker JW., Manson MD., 1997, Maltose-binding protein interacts simultaneously and asymmetrically with both subunits of the Tar chemoreceptor., Mol Microbiol 23(6):1181-91
[10] Gould AD., Telmer PG., Shilton BH., 2009, Stimulation of the maltose transporter ATPase by unliganded maltose binding protein., Biochemistry 48(33):8051-61
[11] Hall JA., Ganesan AK., Chen J., Nikaido H., 1997, Two modes of ligand binding in maltose-binding protein of Escherichia coli. Functional significance in active transport., J Biol Chem 272(28):17615-22
[12] Hall JA., Gehring K., Nikaido H., 1997, Two modes of ligand binding in maltose-binding protein of Escherichia coli. Correlation with the structure of ligands and the structure of binding protein., J Biol Chem 272(28):17605-9
[13] Hall JA., Thorgeirsson TE., Liu J., Shin YK., Nikaido H., 1997, Two modes of ligand binding in maltose-binding protein of Escherichia coli. Electron paramagnetic resonance study of ligand-induced global conformational changes by site-directed spin labeling., J Biol Chem 272(28):17610-4
[14] Hor LI., Shuman HA., 1993, Genetic analysis of periplasmic binding protein dependent transport in Escherichia coli. Each lobe of maltose-binding protein interacts with a different subunit of the MalFGK2 membrane transport complex., J Mol Biol 233(4):659-70
[15] Kainosho M., Torizawa T., Iwashita Y., Terauchi T., Mei Ono A., Guntert P., 2006, Optimal isotope labelling for NMR protein structure determinations., Nature 440(7080):52-7
[16] Kossmann M., Wolff C., Manson MD., 1988, Maltose chemoreceptor of Escherichia coli: interaction of maltose-binding protein and the tar signal transducer., J Bacteriol 170(10):4516-21
[17] Mascarenhas NM., Kastner J., 2013, How maltose influences structural changes to bind to maltose-binding protein: results from umbrella sampling simulation., Proteins 81(2):185-98
[18] Miklos AC., Sumpter M., Zhou HX., 2013, Competitive interactions of ligands and macromolecular crowders with maltose binding protein., PLoS One 8(10):e74969
[19] Quiocho FA., Meador WE., Pflugrath JW., 1979, Preliminary crystallographic data of receptors for transport and chemotaxis in Escherichia coli: D-galactose and maltose-binding proteins., J Mol Biol 133(1):181-4
[20] Sharff AJ., Rodseth LE., Quiocho FA., 1993, Refined 1.8-A structure reveals the mode of binding of beta-cyclodextrin to the maltodextrin binding protein., Biochemistry 32(40):10553-9
[21] Tang C., Schwieters CD., Clore GM., 2007, Open-to-closed transition in apo maltose-binding protein observed by paramagnetic NMR., Nature 449(7165):1078-82
[22] Telmer PG., Shilton BH., 2005, Structural studies of an engineered zinc biosensor reveal an unanticipated mode of zinc binding., J Mol Biol 354(4):829-40
[23] Treptow NA., Shuman HA., 1988, Allele-specific malE mutations that restore interactions between maltose-binding protein and the inner-membrane components of the maltose transport system., J Mol Biol 202(4):809-22
[24] Treptow NA., Shuman HA., 1985, Genetic evidence for substrate and periplasmic-binding-protein recognition by the MalF and MalG proteins, cytoplasmic membrane components of the Escherichia coli maltose transport system., J Bacteriol 163(2):654-60
[25] Walters BT., Mayne L., Hinshaw JR., Sosnick TR., Englander SW., 2013, Folding of a large protein at high structural resolution., Proc Natl Acad Sci U S A 110(47):18898-903
[26] Xu Y., Zheng Y., Fan JS., Yang D., 2006, A new strategy for structure determination of large proteins in solution without deuteration., Nat Methods 3(11):931-7
[27] Ye X., Mayne L., Kan ZY., Englander SW., 2018, Folding of maltose binding protein outside of and in GroEL., Proc Natl Acad Sci U S A 115(3):519-524
[28] Zhang Y., Mannering DE., Davidson AL., Yao N., Manson MD., 1996, Maltose-binding protein containing an interdomain disulfide bridge confers a dominant-negative phenotype for transport and chemotaxis., J Biol Chem 271(30):17881-9
[29] van den Noort M., de Boer M., Poolman B., 2021, Stability of Ligand-induced Protein Conformation Influences Affinity in Maltose-binding Protein., J Mol Biol 433(15):167036