RegulonDB RegulonDB 10.6.3: Gene Form
   

malE gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

malF malE malK MalT MalT MalT CRP CRP Fis CRP CRP MalT MalT CreB Fis terminator anti-terminator anti-anti-terminator malKp malKp malEp malEp

Gene      
Name: malE    Texpresso search in the literature
Synonym(s): ECK4026, EG10554, b4034
Genome position(nucleotides): 4245229 <-- 4246419 Genome Browser
Strand: reverse
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
51.05
External database links:  
ASAP:
ABE-0013200
CGSC:
532
ECHOBASE:
EB0549
ECOCYC:
EG10554
ECOLIHUB:
malE
OU-MICROARRAY:
b4034
REGULONDB:
b4034
STRING:
511145.b4034
M3D: malE
COLOMBOS: malE
PortEco: b4034


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
256 -> 256 W
36 -> 36 W
46 -> 46 L
1 -> 26 MKIKTGARILALSALTTMMFSASALA
27 -> 396 KIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTRITK

 

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: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
molecular_function GO:0005215 - transporter activity
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
External database links:  
DIP:
DIP-31871N
ECOCYC:
MALE-MONOMER
ECOLIWIKI:
b4034
INTERPRO:
IPR006059
INTERPRO:
IPR006060
INTERPRO:
IPR006061
MINT:
P0AEX9
MODBASE:
P0AEX9
PDB:
1A7L
PDB:
1ANF
PDB:
1DMB
PDB:
1HSJ
PDB:
1IUD
PDB:
1JVY
PDB:
1JW4
PDB:
1JW5
PDB:
1LLS
PDB:
1MDP
PDB:
1MDQ
PDB:
1MG1
PDB:
1MH3
PDB:
1MH4
PDB:
1MPB
PDB:
1MPC
PDB:
1MPD
PDB:
1NMU
PDB:
1OMP
PDB:
1R6Z
PDB:
1T0K
PDB:
1Y4C
PDB:
1YTV
PDB:
1ZKB
PDB:
1ez9
PDB:
1ezo
PDB:
1ezp
PDB:
1fqa
PDB:
1fqb
PDB:
1fqc
PDB:
1fqd
PDB:
1jvx
PDB:
1lax
PDB:
1n3w
PDB:
1n3x
PDB:
1nl5
PDB:
1peb
PDB:
1svx
PDB:
1ziu
PDB:
1zjl
PDB:
1zmg
PDB:
2KLF
PDB:
2MV0
PDB:
2N44
PDB:
2N45
PDB:
2NVU
PDB:
2OBG
PDB:
2OK2
PDB:
2VGQ
PDB:
2XZ3
PDB:
2ZXT
PDB:
2d21
PDB:
2h25
PDB:
2r6g
PDB:
2v93
PDB:
3A3C
PDB:
3C4M
PDB:
3CSB
PDB:
3CSG
PDB:
3D4C
PDB:
3D4G
PDB:
3DM0
PDB:
3EF7
PDB:
3EHS
PDB:
3EHT
PDB:
3EHU
PDB:
3F5F
PDB:
3G7V
PDB:
3G7W
PDB:
3H3G
PDB:
3H4Z
PDB:
3HPI
PDB:
3HST
PDB:
3IO4
PDB:
3IO6
PDB:
3IOR
PDB:
3IOT
PDB:
3IOU
PDB:
3IOV
PDB:
3IOW
PDB:
3J9P
PDB:
3KJT
PDB:
3L2J
PDB:
3LBS
PDB:
3LC8
PDB:
3MBP
PDB:
3MP1
PDB:
3MP6
PDB:
3MP8
PDB:
3MQ9
PDB:
3N94
PDB:
3O3U
PDB:
3OAI
PDB:
3OB4
PDB:
3OSQ
PDB:
3OSR
PDB:
3PGF
PDB:
3PUV
PDB:
3PUW
PDB:
3PUX
PDB:
3PUY
PDB:
3PUZ
PDB:
3PV0
PDB:
3PY7
PDB:
3Q25
PDB:
3Q26
PDB:
3Q27
PDB:
3Q28
PDB:
3Q29
PDB:
3RLF
PDB:
3RUM
PDB:
3SER
PDB:
3SES
PDB:
3SET
PDB:
3SEU
PDB:
3SEV
PDB:
3SEW
PDB:
3SEX
PDB:
3SEY
PDB:
3VFJ
PDB:
3W15
PDB:
3WAI
PDB:
3WOA
PDB:
4B3N
PDB:
4BL8
PDB:
4BL9
PDB:
4BLA
PDB:
4BLB
PDB:
4BLD
PDB:
4DXB
PDB:
4DXC
PDB:
4EDQ
PDB:
4EGC
PDB:
4EXK
PDB:
4FE8
PDB:
4FEB
PDB:
4FEC
PDB:
4FED
PDB:
4GIZ
PDB:
4GLI
PDB:
4IFP
PDB:
4IKM
PDB:
4IRL
PDB:
4JBZ
PDB:
4JKM
PDB:
4KEG
PDB:
4KHZ
PDB:
4KI0
PDB:
4KV3
PDB:
4KYC
PDB:
4KYD
PDB:
4KYE
PDB:
4LOG
PDB:
4MBP
PDB:
4N4X
PDB:
4NDZ
PDB:
4NUF
PDB:
4O2X
PDB:
4OGM
PDB:
4PE2
PDB:
4PQK
PDB:
4QSZ
PDB:
4QVH
PDB:
4R0Y
PDB:
4RG5
PDB:
4RWF
PDB:
4RWG
PDB:
4TSM
PDB:
4WJV
PDB:
4WMS
PDB:
4WMT
PDB:
4WMU
PDB:
4WMV
PDB:
4WMW
PDB:
4WMX
PDB:
4WRN
PDB:
4WTH
PDB:
4WVH
PDB:
4XA2
PDB:
4XAJ
PDB:
4XHS
PDB:
4XR8
PDB:
4XZS
PDB:
4XZV
PDB:
5AQ9
PDB:
5AZ6
PDB:
5AZ7
PDB:
5AZ8
PDB:
5AZ9
PDB:
5AZA
PDB:
5B3W
PDB:
5B3X
PDB:
5B3Y
PDB:
5B3Z
PDB:
5BK1
PDB:
5BK2
PDB:
5C7R
PDB:
5CBN
PDB:
5CFV
PDB:
5DFM
PDB:
5DIS
PDB:
5E24
PDB:
5EDU
PDB:
5FIO
PDB:
5FSG
PDB:
5GRU
PDB:
5GS2
PDB:
5GXT
PDB:
5GXV
PDB:
5H7N
PDB:
5H7Q
PDB:
5HZ7
PDB:
5HZV
PDB:
5HZW
PDB:
5I04
PDB:
5I69
PDB:
5IHJ
PDB:
5II5
PDB:
5IIC
PDB:
5IQZ
PDB:
5JJ4
PDB:
5JST
PDB:
5JTQ
PDB:
5JTR
PDB:
5LDF
PDB:
5M13
PDB:
5M14
PDB:
5M15
PDB:
5OSQ
PDB:
5T03
PDB:
5T05
PDB:
5T0A
PDB:
5TTD
PDB:
5VAW
PDB:
5WPZ
PDB:
5WQ6
PDB:
5Z0R
PDB:
5Z0V
PDB:
5ZCA
PDB:
5ZR0
PDB:
6APX
PDB:
6D65
PDB:
6D66
PDB:
6D67
PDB:
6DM8
PFAM:
PF13416
PRIDE:
P0AEX9
PRINTS:
PR00181
PRODB:
PRO_000023147
PROSITE:
PS01037
PROTEINMODELPORTAL:
P0AEX9
REFSEQ:
NP_418458
SMR:
P0AEX9
SWISSMODEL:
P0AEX9
UNIPROT:
P0AEX9


Operon      
Name: malEFG         
Operon arrangement:
Transcription unit        Promoter
malEFG


Transcriptional Regulation      
Display Regulation             
Activated by: CRP, MalT, Fis
Repressed by: CreB
Growth Conditions:

[1] 

C: Escherichia coli| 0.1 MPa
E: Escherichia coli| maltose 0.2%| 0.1 MPa

[2] 

C: Escherichia coli| maltose 0.2%| 0.1 MPa
E: Escherichia coli| maltose 0.2%| 10 to 40 MPa



Elements in the selected gene context region unrelated to any object in RegulonDB      

  Type Name Post Left Post Right Strand Notes Evidence (Confirmed, Strong, Weak) References


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


RegulonDB