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P0AEX9 (MALE_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Maltose-binding periplasmic protein
Alternative name(s):
MBP
MMBP
Maltodextrin-binding protein
Gene names
Name:malE
Ordered Locus Names:b4034, JW3994
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length396 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.

Subcellular location

Periplasm.

Induction

Permanently repressed by cold shock in a PNPase-dependent fashion. Ref.11

Sequence similarities

Belongs to the bacterial solute-binding protein 1 family.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Ref.8 Ref.9
Chain27 – 396370Maltose-binding periplasmic protein
PRO_0000031694

Experimental info

Sequence conflict361W → A AA sequence Ref.8
Sequence conflict461L → H in CAA23581. Ref.5

Secondary structure

.............................................................................. 396
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0AEX9 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: A4C1B3C1777ADE47

FASTA39643,388
        10         20         30         40         50         60 
MKIKTGARIL ALSALTTMMF SASALAKIEE GKLVIWINGD KGYNGLAEVG KKFEKDTGIK 

        70         80         90        100        110        120 
VTVEHPDKLE EKFPQVAATG DGPDIIFWAH DRFGGYAQSG LLAEITPDKA FQDKLYPFTW 

       130        140        150        160        170        180 
DAVRYNGKLI AYPIAVEALS LIYNKDLLPN PPKTWEEIPA LDKELKAKGK SALMFNLQEP 

       190        200        210        220        230        240 
YFTWPLIAAD GGYAFKYENG KYDIKDVGVD NAGAKAGLTF LVDLIKNKHM NADTDYSIAE 

       250        260        270        280        290        300 
AAFNKGETAM TINGPWAWSN IDTSKVNYGV TVLPTFKGQP SKPFVGVLSA GINAASPNKE 

       310        320        330        340        350        360 
LAKEFLENYL LTDEGLEAVN KDKPLGAVAL KSYEEELAKD PRIAATMENA QKGEIMPNIP 

       370        380        390 
QMSAFWYAVR TAVINAASGR QTVDEALKDA QTRITK 

« Hide

References

« Hide 'large scale' references
[1]"Sequences of the malE gene and of its product, the maltose-binding protein of Escherichia coli K12."
Duplay P., Bedouelle H., Fowler A., Zabin I., Saurin W., Hofnung M.
J. Biol. Chem. 259:10606-10613(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: K12.
[2]"Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
Nucleic Acids Res. 21:5408-5417(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"A DNA sequence containing the control regions of the malEFG and malK-lamB operons in Escherichia coli K12."
Bedouelle H., Hofnung M.
Mol. Gen. Genet. 185:82-87(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-48.
[6]"Promoters of the malEFG and malK-lamB operons in Escherichia coli K12."
Bedouelle H., Schmeissner U., Hofnung M., Rosenberg M.
J. Mol. Biol. 161:519-531(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32.
[7]"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."
Froshauer S., Beckwith J.
J. Biol. Chem. 259:10896-10903(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 392-396.
[8]"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
Link A.J., Robison K., Church G.M.
Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 27-38.
Strain: K12 / EMG2.
[9]"Protein identification with N and C-terminal sequence tags in proteome projects."
Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L., Hochstrasser D.F.
J. Mol. Biol. 278:599-608(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 27-30.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[10]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[11]"Changes in Escherichia coli transcriptome during acclimatization at low temperature."
Polissi A., De Laurentis W., Zangrossi S., Briani F., Longhi V., Pesole G., Deho G.
Res. Microbiol. 154:573-580(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
Strain: K12 / MG1655 / ATCC 47076.
[12]"The 2.3-A resolution structure of the maltose-or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis."
Spurlino J.C., Lu G.-Y., Quiocho F.A.
J. Biol. Chem. 266:5202-5219(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[13]"Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis."
Sharff A.J., Rodseth L.E., Spurlino J.C., Quiocho F.A.
Biochemistry 31:10657-10663(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[14]"Extensive features of tight oligosaccharide binding revealed in high-resolution structures of the maltodextrin transport/chemosensory receptor."
Quiocho F.A., Spurlino J.C., Rodseth L.E.
Structure 5:997-1015(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
[15]"Redirecting the substrate specificity of heparan sulfate 2-O-sulfotransferase by structurally guided mutagenesis."
Bethea H.N., Xu D., Liu J., Pedersen L.C.
Proc. Natl. Acad. Sci. U.S.A. 105:18724-18729(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 27-392 IN COMPLEX WITH CHICKEN HS2ST1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V00303 Genomic DNA. Translation: CAA23581.1.
U00006 Genomic DNA. Translation: AAC43128.1.
U00096 Genomic DNA. Translation: AAC77004.1.
AP009048 Genomic DNA. Translation: BAE78036.1.
J01648 Genomic DNA. Translation: AAB59056.1.
M16181 Genomic DNA. Translation: AAA24102.1.
M12635 Genomic DNA. Translation: AAA24123.1.
M12647 Genomic DNA. Translation: AAA24135.1.
M12650 Genomic DNA. Translation: AAA24138.1.
M12653 Genomic DNA. Translation: AAA24115.1.
PIRJGECM. A03428.
RefSeqNP_418458.1. NC_000913.3.
YP_492177.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A7LX-ray2.90A/B/C27-389[»]
1ANFX-ray1.67A27-396[»]
1DMBX-ray1.80A27-396[»]
1EZ9X-ray1.90A/B27-396[»]
1EZONMR-A29-396[»]
1EZPNMR-A29-396[»]
1FQAX-ray1.90A28-396[»]
1FQBX-ray1.90A28-396[»]
1FQCX-ray2.30A28-396[»]
1FQDX-ray2.30A28-396[»]
1HSJX-ray2.30A/B27-396[»]
1IUDX-ray2.70A27-396[»]
1JVXX-ray2.50A27-396[»]
1JVYX-ray1.90A27-396[»]
1JW4X-ray2.00A27-396[»]
1JW5X-ray2.00A27-396[»]
1LAXX-ray1.85A/C27-396[»]
1LLSX-ray1.80A27-396[»]
1MDPX-ray2.301/227-396[»]
1MDQX-ray1.90A27-396[»]
1MG1X-ray2.50A31-392[»]
1MH3X-ray2.10A27-392[»]
1MH4X-ray2.30A27-392[»]
1MPBX-ray2.00A27-396[»]
1MPCX-ray2.10A27-396[»]
1MPDX-ray2.30A27-396[»]
1N3WX-ray2.60A27-396[»]
1N3XX-ray2.50A27-396[»]
1NL5X-ray2.10A27-396[»]
1NMUX-ray2.31A/C27-392[»]
1OMPX-ray1.80A27-396[»]
1PEBX-ray2.60A27-396[»]
1R6ZX-ray2.80A/P/Z27-392[»]
1SVXX-ray2.24B29-392[»]
1T0KX-ray3.24A29-392[»]
1Y4CX-ray1.90A27-392[»]
1YTVX-ray1.80A/B27-392[»]
1ZIUX-ray2.00A27-396[»]
1ZJLX-ray2.00A27-396[»]
1ZKBX-ray2.20A27-396[»]
1ZMGX-ray2.50A27-396[»]
2D21NMR-A27-396[»]
2H25NMR-A29-396[»]
2KLFNMR-A29-396[»]
2NVUX-ray2.80B25-392[»]
2OBGX-ray2.35A31-396[»]
2OK2X-ray2.00A/B28-392[»]
2R6GX-ray2.80E27-396[»]
2V93NMR-A27-396[»]
2VGQX-ray2.10A27-392[»]
2XZ3X-ray1.95A27-392[»]
2ZXTX-ray3.00A27-392[»]
3A3CX-ray2.50A29-392[»]
3C4MX-ray1.95A/B26-392[»]
3CSBX-ray2.00A31-396[»]
3CSGX-ray1.80A31-396[»]
3DM0X-ray2.40A27-392[»]
3EHSX-ray2.76A26-392[»]
3EHTX-ray3.40A26-392[»]
3EHUX-ray1.96A/B26-392[»]
3F5FX-ray2.65A27-392[»]
3G7VX-ray1.86A/B/C/D27-392[»]
3G7WX-ray1.75A27-392[»]
3H3GX-ray1.94A26-392[»]
3H4ZX-ray2.35A/B/C27-392[»]
3HPIX-ray2.00A/B26-396[»]
3HSTX-ray2.25A/C27-392[»]
3IO4X-ray3.63A/B/C27-392[»]
3IO6X-ray3.70A/B/C27-384[»]
3IORX-ray3.60A/B/C27-392[»]
3IOTX-ray3.50A/B/C27-392[»]
3IOUX-ray3.70A/B/C27-392[»]
3IOVX-ray3.70A/B/C27-392[»]
3IOWX-ray3.50A/B/C27-392[»]
3KJTX-ray1.50A26-396[»]
3L2JX-ray3.24A/B29-392[»]
3LBSX-ray2.15A/B29-390[»]
3LC8X-ray2.00A/B29-390[»]
3MBPX-ray1.70A27-396[»]
3MP1X-ray2.60A27-392[»]
3MP6X-ray1.48A27-392[»]
3MP8X-ray1.92A27-392[»]
3MQ9X-ray2.80A/B/C/D/E/F/G/H27-395[»]
3N94X-ray1.80A26-392[»]
3O3UX-ray1.50N28-384[»]
3OAIX-ray2.10A/B27-392[»]
3OSQX-ray1.90A27-396[»]
3OSRX-ray2.00A/B27-396[»]
3PGFX-ray2.10A27-392[»]
3PUVX-ray2.40E27-396[»]
3PUWX-ray2.30E27-396[»]
3PUXX-ray2.30E27-396[»]
3PUYX-ray3.10E27-396[»]
3PUZX-ray2.90E27-396[»]
3PV0X-ray3.10E27-396[»]
3PY7X-ray2.29A27-392[»]
3Q25X-ray1.90A27-392[»]
3Q26X-ray1.54A27-392[»]
3Q27X-ray1.30A27-392[»]
3Q28X-ray1.60A27-392[»]
3Q29X-ray2.30A/C27-392[»]
3RLFX-ray2.20E27-396[»]
3RUMX-ray1.85A27-392[»]
3SERX-ray2.35A/C27-392[»]
3SESX-ray1.90A/C27-392[»]
3SETX-ray1.90A/C27-392[»]
3SEUX-ray1.85A27-392[»]
3SEVX-ray3.05A/C/E27-392[»]
3SEWX-ray1.55A27-392[»]
3SEXX-ray1.95A/C27-392[»]
3SEYX-ray1.85A/C/E27-392[»]
3VFJX-ray2.05A27-392[»]
3W15X-ray1.80C27-396[»]
3WAIX-ray1.90A27-392[»]
4B3NX-ray3.30A/B27-395[»]
4BL8X-ray3.04A/B27-393[»]
4BL9X-ray2.80A/B/C/D27-393[»]
4BLAX-ray3.50A/B/C/D27-393[»]
4BLBX-ray2.80A/B/C/D27-393[»]
4BLDX-ray2.80A/B/C/D27-393[»]
4DXBX-ray2.29A/B27-396[»]
4DXCX-ray2.30A27-396[»]
4EDQX-ray1.64A/B27-392[»]
4EGCX-ray1.99A27-392[»]
4EXKX-ray1.28A26-392[»]
4FE8X-ray3.00A/B/C27-384[»]
4FEBX-ray2.80A/B/C27-384[»]
4FECX-ray3.00A/B/C27-384[»]
4FEDX-ray2.81A/B/C27-384[»]
4GIZX-ray2.55A/B27-392[»]
4GLIX-ray1.90A27-395[»]
4IFPX-ray1.99A/B/C27-384[»]
4IKMX-ray2.46A27-392[»]
4IRLX-ray1.47A/B/C27-384[»]
4JBZX-ray2.40A/B/C27-392[»]
4KHZX-ray2.90E27-396[»]
4KI0X-ray2.38E27-396[»]
4KYCX-ray1.95A27-388[»]
4KYDX-ray2.21A/B27-388[»]
4KYEX-ray2.60A27-388[»]
4MBPX-ray1.70A27-396[»]
ProteinModelPortalP0AEX9.
SMRP0AEX9. Positions 27-392.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-31871N.
IntActP0AEX9. 10 interactions.
STRING511145.b4034.

Protein family/group databases

TCDB3.A.1.1.1. the atp-binding cassette (abc) superfamily.

2D gel databases

SWISS-2DPAGEP0AEX9.

Proteomic databases

PaxDbP0AEX9.
PRIDEP0AEX9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC77004; AAC77004; b4034.
BAE78036; BAE78036; BAE78036.
GeneID12934071.
948538.
KEGGecj:Y75_p3921.
eco:b4034.
PATRIC32123601. VBIEscCol129921_4149.

Organism-specific databases

EchoBASEEB0549.
EcoGeneEG10554. malE.

Phylogenomic databases

eggNOGCOG2182.
HOGENOMHOG000055250.
KOK10108.
OMANDSDYAS.
OrthoDBEOG6CCH2B.
PhylomeDBP0AEX9.
ProtClustDBPRK09474.

Enzyme and pathway databases

BioCycEcoCyc:MALE-MONOMER.
ECOL316407:JW3994-MONOMER.

Gene expression databases

GenevestigatorP0AEX9.

Family and domain databases

InterProIPR006060. Maltose-bd.
IPR006059. Solute-bd_1_bac.
IPR006061. Solute-bd_1_bac_CS.
[Graphical view]
PfamPF01547. SBP_bac_1. 1 hit.
[Graphical view]
PRINTSPR00181. MALTOSEBP.
PROSITEPS01037. SBP_BACTERIAL_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0AEX9.
PROP0AEX9.

Entry information

Entry nameMALE_ECOLI
AccessionPrimary (citable) accession number: P0AEX9
Secondary accession number(s): P02928, Q2M6S0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 16, 2014
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene