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P0AEX9

- MALE_ECOLI

UniProt

P0AEX9 - MALE_ECOLI

Protein

Maltose-binding periplasmic protein

Gene

malE

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    Functioni

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

    GO - Molecular functioni

    1. maltose binding Source: EcoCyc
    2. maltose transmembrane transporter activity Source: InterPro
    3. protein binding Source: IntAct
    4. transporter activity Source: EcoliWiki

    GO - Biological processi

    1. carbohydrate transport Source: EcoliWiki
    2. cell chemotaxis Source: EcoCyc
    3. cellular response to DNA damage stimulus Source: EcoliWiki
    4. detection of maltose stimulus Source: EcoCyc
    5. maltodextrin transport Source: EcoCyc
    6. maltose transport Source: EcoCyc
    7. transport Source: EcoliWiki

    Keywords - Biological processi

    Sugar transport, Transport

    Enzyme and pathway databases

    BioCyciEcoCyc:MALE-MONOMER.
    ECOL316407:JW3994-MONOMER.
    MetaCyc:MALE-MONOMER.

    Protein family/group databases

    TCDBi3.A.1.1.1. the atp-binding cassette (abc) superfamily.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Maltose-binding periplasmic protein
    Alternative name(s):
    MBP
    MMBP
    Maltodextrin-binding protein
    Gene namesi
    Name:malE
    Ordered Locus Names:b4034, JW3994
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10554. malE.

    Subcellular locationi

    GO - Cellular componenti

    1. ATP-binding cassette (ABC) transporter complex Source: EcoliWiki
    2. ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing Source: EcoCyc
    3. maltose transport complex Source: EcoCyc
    4. outer membrane-bounded periplasmic space Source: EcoCyc
    5. periplasmic space Source: EcoliWiki

    Keywords - Cellular componenti

    Periplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 26262 PublicationsAdd
    BLAST
    Chaini27 – 396370Maltose-binding periplasmic proteinPRO_0000031694Add
    BLAST

    Proteomic databases

    PaxDbiP0AEX9.
    PRIDEiP0AEX9.

    2D gel databases

    SWISS-2DPAGEP0AEX9.

    Expressioni

    Inductioni

    Permanently repressed by cold shock in a PNPase-dependent fashion.1 Publication

    Gene expression databases

    GenevestigatoriP0AEX9.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    groLP0A6F53EBI-369910,EBI-543750
    malFP029162EBI-369910,EBI-1118919

    Protein-protein interaction databases

    DIPiDIP-31871N.
    IntActiP0AEX9. 10 interactions.
    STRINGi511145.b4034.

    Structurei

    Secondary structure

    1
    396
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni28 – 314
    Beta strandi32 – 365
    Helixi39 – 413
    Helixi43 – 5715
    Beta strandi60 – 645
    Helixi69 – 768
    Turni77 – 804
    Beta strandi84 – 896
    Helixi90 – 923
    Helixi93 – 986
    Beta strandi99 – 1013
    Helixi109 – 1124
    Helixi117 – 1226
    Beta strandi123 – 1253
    Beta strandi126 – 1294
    Beta strandi131 – 1377
    Beta strandi140 – 1445
    Turni145 – 1473
    Beta strandi148 – 1503
    Beta strandi153 – 1553
    Helixi158 – 1669
    Turni167 – 1693
    Beta strandi171 – 1733
    Beta strandi177 – 1793
    Helixi180 – 18910
    Beta strandi193 – 1986
    Beta strandi201 – 2088
    Beta strandi209 – 2113
    Helixi212 – 22615
    Beta strandi227 – 2304
    Helixi236 – 2449
    Beta strandi248 – 2536
    Helixi255 – 2573
    Helixi258 – 2636
    Beta strandi268 – 2714
    Beta strandi275 – 2795
    Beta strandi284 – 29310
    Beta strandi294 – 2974
    Helixi299 – 30810
    Turni309 – 3113
    Helixi313 – 32210
    Beta strandi327 – 3304
    Helixi331 – 3377
    Beta strandi338 – 3403
    Helixi341 – 35212
    Beta strandi353 – 3553
    Helixi362 – 37716
    Beta strandi379 – 3813
    Helixi383 – 39210

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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-A27-396[»]
    2KLFNMR-A27-396[»]
    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-ray2.40A27-387[»]
    3EHSX-ray2.76A26-392[»]
    3EHTX-ray3.40A26-392[»]
    3EHUX-ray1.96A/B26-392[»]
    3F5FX-ray2.65A27-387[»]
    3G7VX-ray1.86A/B/C/D27-392[»]
    3G7WX-ray1.75A27-392[»]
    3H3GX-ray1.94A26-392[»]
    3H4ZX-ray2.35A/B/C27-387[»]
    3HPIX-ray2.00A/B27-396[»]
    3HSTX-ray2.25A/C27-392[»]
    3IO4X-ray3.63A/B/C27-384[»]
    3IO6X-ray3.70A/B/C27-384[»]
    3IORX-ray3.60A/B/C27-384[»]
    3IOTX-ray3.50A/B/C27-384[»]
    3IOUX-ray3.70A/B/C27-384[»]
    3IOVX-ray3.70A/B/C27-384[»]
    3IOWX-ray3.50A/B/C27-384[»]
    3KJTX-ray1.50A27-396[»]
    3L2JX-ray3.24A/B29-392[»]
    3LBSX-ray2.15A/B29-390[»]
    3LC8X-ray2.00A/B29-390[»]
    3MBPX-ray1.70A27-396[»]
    3MP1X-ray2.60A27-387[»]
    3MP6X-ray1.48A27-387[»]
    3MP8X-ray1.92A27-387[»]
    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-ray2.10A27-393[»]
    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/C27-384[»]
    3SESX-ray1.90A/C27-384[»]
    3SETX-ray1.90A/C27-384[»]
    3SEUX-ray1.85A27-384[»]
    3SEVX-ray3.05A/C/E27-384[»]
    3SEWX-ray1.55A27-384[»]
    3SEXX-ray1.95A/C27-384[»]
    3SEYX-ray1.85A/C/E27-384[»]
    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/B27-384[»]
    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[»]
    4KEGX-ray2.50A27-387[»]
    4KHZX-ray2.90E27-396[»]
    4KI0X-ray2.38E27-396[»]
    4KV3X-ray2.20A/B27-392[»]
    4KYCX-ray1.95A27-392[»]
    4KYDX-ray2.21A/B27-392[»]
    4KYEX-ray2.60A27-392[»]
    4MBPX-ray1.70A27-396[»]
    4NDZX-ray3.45A/B/C/D/E/F27-393[»]
    ProteinModelPortaliP0AEX9.
    SMRiP0AEX9. Positions 27-392.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0AEX9.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2182.
    HOGENOMiHOG000055250.
    KOiK10108.
    OMAiDAVRYDG.
    OrthoDBiEOG6CCH2B.
    PhylomeDBiP0AEX9.

    Family and domain databases

    InterProiIPR006060. Maltose-bd.
    IPR006059. Solute-bd_1_bac.
    IPR006061. Solute-bd_1_bac_CS.
    [Graphical view]
    PfamiPF01547. SBP_bac_1. 1 hit.
    [Graphical view]
    PRINTSiPR00181. MALTOSEBP.
    PROSITEiPS01037. SBP_BACTERIAL_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P0AEX9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKIKTGARIL ALSALTTMMF SASALAKIEE GKLVIWINGD KGYNGLAEVG    50
    KKFEKDTGIK VTVEHPDKLE EKFPQVAATG DGPDIIFWAH DRFGGYAQSG 100
    LLAEITPDKA FQDKLYPFTW DAVRYNGKLI AYPIAVEALS LIYNKDLLPN 150
    PPKTWEEIPA LDKELKAKGK SALMFNLQEP YFTWPLIAAD GGYAFKYENG 200
    KYDIKDVGVD NAGAKAGLTF LVDLIKNKHM NADTDYSIAE AAFNKGETAM 250
    TINGPWAWSN IDTSKVNYGV TVLPTFKGQP SKPFVGVLSA GINAASPNKE 300
    LAKEFLENYL LTDEGLEAVN KDKPLGAVAL KSYEEELAKD PRIAATMENA 350
    QKGEIMPNIP QMSAFWYAVR TAVINAASGR QTVDEALKDA QTRITK 396
    Length:396
    Mass (Da):43,388
    Last modified:July 21, 1986 - v1
    Checksum:iA4C1B3C1777ADE47
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti36 – 361W → A AA sequence (PubMed:9298646)Curated
    Sequence conflicti46 – 461L → H in CAA23581. (PubMed:6283312)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    PIRiA03428. JGECM.
    RefSeqiNP_418458.1. NC_000913.3.
    YP_492177.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC77004; AAC77004; b4034.
    BAE78036; BAE78036; BAE78036.
    GeneIDi12934071.
    948538.
    KEGGiecj:Y75_p3921.
    eco:b4034.
    PATRICi32123601. VBIEscCol129921_4149.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    PIRi A03428. JGECM.
    RefSeqi NP_418458.1. NC_000913.3.
    YP_492177.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A7L X-ray 2.90 A/B/C 27-389 [» ]
    1ANF X-ray 1.67 A 27-396 [» ]
    1DMB X-ray 1.80 A 27-396 [» ]
    1EZ9 X-ray 1.90 A/B 27-396 [» ]
    1EZO NMR - A 29-396 [» ]
    1EZP NMR - A 29-396 [» ]
    1FQA X-ray 1.90 A 28-396 [» ]
    1FQB X-ray 1.90 A 28-396 [» ]
    1FQC X-ray 2.30 A 28-396 [» ]
    1FQD X-ray 2.30 A 28-396 [» ]
    1HSJ X-ray 2.30 A/B 27-396 [» ]
    1IUD X-ray 2.70 A 27-396 [» ]
    1JVX X-ray 2.50 A 27-396 [» ]
    1JVY X-ray 1.90 A 27-396 [» ]
    1JW4 X-ray 2.00 A 27-396 [» ]
    1JW5 X-ray 2.00 A 27-396 [» ]
    1LAX X-ray 1.85 A/C 27-396 [» ]
    1LLS X-ray 1.80 A 27-396 [» ]
    1MDP X-ray 2.30 1/2 27-396 [» ]
    1MDQ X-ray 1.90 A 27-396 [» ]
    1MG1 X-ray 2.50 A 31-392 [» ]
    1MH3 X-ray 2.10 A 27-392 [» ]
    1MH4 X-ray 2.30 A 27-392 [» ]
    1MPB X-ray 2.00 A 27-396 [» ]
    1MPC X-ray 2.10 A 27-396 [» ]
    1MPD X-ray 2.30 A 27-396 [» ]
    1N3W X-ray 2.60 A 27-396 [» ]
    1N3X X-ray 2.50 A 27-396 [» ]
    1NL5 X-ray 2.10 A 27-396 [» ]
    1NMU X-ray 2.31 A/C 27-392 [» ]
    1OMP X-ray 1.80 A 27-396 [» ]
    1PEB X-ray 2.60 A 27-396 [» ]
    1R6Z X-ray 2.80 A/P/Z 27-392 [» ]
    1SVX X-ray 2.24 B 29-392 [» ]
    1T0K X-ray 3.24 A 29-392 [» ]
    1Y4C X-ray 1.90 A 27-392 [» ]
    1YTV X-ray 1.80 A/B 27-392 [» ]
    1ZIU X-ray 2.00 A 27-396 [» ]
    1ZJL X-ray 2.00 A 27-396 [» ]
    1ZKB X-ray 2.20 A 27-396 [» ]
    1ZMG X-ray 2.50 A 27-396 [» ]
    2D21 NMR - A 27-396 [» ]
    2H25 NMR - A 27-396 [» ]
    2KLF NMR - A 27-396 [» ]
    2NVU X-ray 2.80 B 25-392 [» ]
    2OBG X-ray 2.35 A 31-396 [» ]
    2OK2 X-ray 2.00 A/B 28-392 [» ]
    2R6G X-ray 2.80 E 27-396 [» ]
    2V93 NMR - A 27-396 [» ]
    2VGQ X-ray 2.10 A 27-392 [» ]
    2XZ3 X-ray 1.95 A 27-392 [» ]
    2ZXT X-ray 3.00 A 27-392 [» ]
    3A3C X-ray 2.50 A 29-392 [» ]
    3C4M X-ray 1.95 A/B 26-392 [» ]
    3CSB X-ray 2.00 A 31-396 [» ]
    3CSG X-ray 1.80 A 31-396 [» ]
    3DM0 X-ray 2.40 A 27-387 [» ]
    3EHS X-ray 2.76 A 26-392 [» ]
    3EHT X-ray 3.40 A 26-392 [» ]
    3EHU X-ray 1.96 A/B 26-392 [» ]
    3F5F X-ray 2.65 A 27-387 [» ]
    3G7V X-ray 1.86 A/B/C/D 27-392 [» ]
    3G7W X-ray 1.75 A 27-392 [» ]
    3H3G X-ray 1.94 A 26-392 [» ]
    3H4Z X-ray 2.35 A/B/C 27-387 [» ]
    3HPI X-ray 2.00 A/B 27-396 [» ]
    3HST X-ray 2.25 A/C 27-392 [» ]
    3IO4 X-ray 3.63 A/B/C 27-384 [» ]
    3IO6 X-ray 3.70 A/B/C 27-384 [» ]
    3IOR X-ray 3.60 A/B/C 27-384 [» ]
    3IOT X-ray 3.50 A/B/C 27-384 [» ]
    3IOU X-ray 3.70 A/B/C 27-384 [» ]
    3IOV X-ray 3.70 A/B/C 27-384 [» ]
    3IOW X-ray 3.50 A/B/C 27-384 [» ]
    3KJT X-ray 1.50 A 27-396 [» ]
    3L2J X-ray 3.24 A/B 29-392 [» ]
    3LBS X-ray 2.15 A/B 29-390 [» ]
    3LC8 X-ray 2.00 A/B 29-390 [» ]
    3MBP X-ray 1.70 A 27-396 [» ]
    3MP1 X-ray 2.60 A 27-387 [» ]
    3MP6 X-ray 1.48 A 27-387 [» ]
    3MP8 X-ray 1.92 A 27-387 [» ]
    3MQ9 X-ray 2.80 A/B/C/D/E/F/G/H 27-395 [» ]
    3N94 X-ray 1.80 A 26-392 [» ]
    3O3U X-ray 1.50 N 28-384 [» ]
    3OAI X-ray 2.10 A/B 27-392 [» ]
    3OSQ X-ray 1.90 A 27-396 [» ]
    3OSR X-ray 2.00 A/B 27-396 [» ]
    3PGF X-ray 2.10 A 27-393 [» ]
    3PUV X-ray 2.40 E 27-396 [» ]
    3PUW X-ray 2.30 E 27-396 [» ]
    3PUX X-ray 2.30 E 27-396 [» ]
    3PUY X-ray 3.10 E 27-396 [» ]
    3PUZ X-ray 2.90 E 27-396 [» ]
    3PV0 X-ray 3.10 E 27-396 [» ]
    3PY7 X-ray 2.29 A 27-392 [» ]
    3Q25 X-ray 1.90 A 27-392 [» ]
    3Q26 X-ray 1.54 A 27-392 [» ]
    3Q27 X-ray 1.30 A 27-392 [» ]
    3Q28 X-ray 1.60 A 27-392 [» ]
    3Q29 X-ray 2.30 A/C 27-392 [» ]
    3RLF X-ray 2.20 E 27-396 [» ]
    3RUM X-ray 1.85 A 27-392 [» ]
    3SER X-ray 2.35 A/C 27-384 [» ]
    3SES X-ray 1.90 A/C 27-384 [» ]
    3SET X-ray 1.90 A/C 27-384 [» ]
    3SEU X-ray 1.85 A 27-384 [» ]
    3SEV X-ray 3.05 A/C/E 27-384 [» ]
    3SEW X-ray 1.55 A 27-384 [» ]
    3SEX X-ray 1.95 A/C 27-384 [» ]
    3SEY X-ray 1.85 A/C/E 27-384 [» ]
    3VFJ X-ray 2.05 A 27-392 [» ]
    3W15 X-ray 1.80 C 27-396 [» ]
    3WAI X-ray 1.90 A 27-392 [» ]
    4B3N X-ray 3.30 A/B 27-395 [» ]
    4BL8 X-ray 3.04 A/B 27-393 [» ]
    4BL9 X-ray 2.80 A/B/C/D 27-393 [» ]
    4BLA X-ray 3.50 A/B/C/D 27-393 [» ]
    4BLB X-ray 2.80 A/B/C/D 27-393 [» ]
    4BLD X-ray 2.80 A/B/C/D 27-393 [» ]
    4DXB X-ray 2.29 A/B 27-396 [» ]
    4DXC X-ray 2.30 A 27-396 [» ]
    4EDQ X-ray 1.64 A/B 27-384 [» ]
    4EGC X-ray 1.99 A 27-392 [» ]
    4EXK X-ray 1.28 A 26-392 [» ]
    4FE8 X-ray 3.00 A/B/C 27-384 [» ]
    4FEB X-ray 2.80 A/B/C 27-384 [» ]
    4FEC X-ray 3.00 A/B/C 27-384 [» ]
    4FED X-ray 2.81 A/B/C 27-384 [» ]
    4GIZ X-ray 2.55 A/B 27-392 [» ]
    4GLI X-ray 1.90 A 27-395 [» ]
    4IFP X-ray 1.99 A/B/C 27-384 [» ]
    4IKM X-ray 2.46 A 27-392 [» ]
    4IRL X-ray 1.47 A/B/C 27-384 [» ]
    4JBZ X-ray 2.40 A/B/C 27-392 [» ]
    4KEG X-ray 2.50 A 27-387 [» ]
    4KHZ X-ray 2.90 E 27-396 [» ]
    4KI0 X-ray 2.38 E 27-396 [» ]
    4KV3 X-ray 2.20 A/B 27-392 [» ]
    4KYC X-ray 1.95 A 27-392 [» ]
    4KYD X-ray 2.21 A/B 27-392 [» ]
    4KYE X-ray 2.60 A 27-392 [» ]
    4MBP X-ray 1.70 A 27-396 [» ]
    4NDZ X-ray 3.45 A/B/C/D/E/F 27-393 [» ]
    ProteinModelPortali P0AEX9.
    SMRi P0AEX9. Positions 27-392.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-31871N.
    IntActi P0AEX9. 10 interactions.
    STRINGi 511145.b4034.

    Protein family/group databases

    TCDBi 3.A.1.1.1. the atp-binding cassette (abc) superfamily.

    2D gel databases

    SWISS-2DPAGE P0AEX9.

    Proteomic databases

    PaxDbi P0AEX9.
    PRIDEi P0AEX9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC77004 ; AAC77004 ; b4034 .
    BAE78036 ; BAE78036 ; BAE78036 .
    GeneIDi 12934071.
    948538.
    KEGGi ecj:Y75_p3921.
    eco:b4034.
    PATRICi 32123601. VBIEscCol129921_4149.

    Organism-specific databases

    EchoBASEi EB0549.
    EcoGenei EG10554. malE.

    Phylogenomic databases

    eggNOGi COG2182.
    HOGENOMi HOG000055250.
    KOi K10108.
    OMAi DAVRYDG.
    OrthoDBi EOG6CCH2B.
    PhylomeDBi P0AEX9.

    Enzyme and pathway databases

    BioCyci EcoCyc:MALE-MONOMER.
    ECOL316407:JW3994-MONOMER.
    MetaCyc:MALE-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0AEX9.
    PROi P0AEX9.

    Gene expression databases

    Genevestigatori P0AEX9.

    Family and domain databases

    InterProi IPR006060. Maltose-bd.
    IPR006059. Solute-bd_1_bac.
    IPR006061. Solute-bd_1_bac_CS.
    [Graphical view ]
    Pfami PF01547. SBP_bac_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00181. MALTOSEBP.
    PROSITEi PS01037. SBP_BACTERIAL_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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. 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.

    Entry informationi

    Entry nameiMALE_ECOLI
    AccessioniPrimary (citable) accession number: P0AEX9
    Secondary accession number(s): P02928, Q2M6S0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 98 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3