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Protein

Maltose-binding periplasmic protein

Gene

malE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. 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
Complete GO annotation...

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
Complete GO annotation...

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

BioGridi852832. 1 interaction.
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 – 314Combined sources
Beta strandi32 – 365Combined sources
Helixi39 – 413Combined sources
Helixi43 – 5715Combined sources
Beta strandi60 – 645Combined sources
Helixi69 – 768Combined sources
Turni77 – 804Combined sources
Beta strandi84 – 896Combined sources
Helixi90 – 923Combined sources
Helixi93 – 986Combined sources
Beta strandi99 – 1013Combined sources
Helixi109 – 1124Combined sources
Helixi117 – 1226Combined sources
Beta strandi123 – 1253Combined sources
Beta strandi126 – 1294Combined sources
Beta strandi131 – 1377Combined sources
Beta strandi140 – 1445Combined sources
Turni145 – 1473Combined sources
Beta strandi148 – 1503Combined sources
Beta strandi153 – 1553Combined sources
Helixi158 – 1669Combined sources
Turni167 – 1693Combined sources
Beta strandi171 – 1733Combined sources
Beta strandi177 – 1793Combined sources
Helixi180 – 18910Combined sources
Beta strandi193 – 1986Combined sources
Beta strandi201 – 2088Combined sources
Beta strandi209 – 2113Combined sources
Helixi212 – 22615Combined sources
Beta strandi227 – 2304Combined sources
Helixi236 – 2449Combined sources
Beta strandi248 – 2536Combined sources
Helixi255 – 2573Combined sources
Helixi258 – 2636Combined sources
Beta strandi268 – 2714Combined sources
Beta strandi275 – 2795Combined sources
Beta strandi284 – 29310Combined sources
Beta strandi294 – 2974Combined sources
Helixi299 – 30810Combined sources
Turni309 – 3113Combined sources
Helixi313 – 32210Combined sources
Beta strandi327 – 3304Combined sources
Helixi331 – 3377Combined sources
Beta strandi338 – 3403Combined sources
Helixi341 – 35212Combined sources
Beta strandi353 – 3553Combined sources
Helixi362 – 37716Combined sources
Beta strandi379 – 3813Combined sources
Helixi383 – 39210Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
2MV0NMR-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[»]
4JKMX-ray2.26C/D27-392[»]
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[»]
4N4XX-ray2.50A27-387[»]
4NDZX-ray3.45A/B/C/D/E/F27-393[»]
4R0YX-ray2.00A/B27-387[»]
4WJVX-ray3.20E/F/G/H27-393[»]
ProteinModelPortaliP0AEX9.
SMRiP0AEX9. Positions 27-392.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AEX9.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2182.
HOGENOMiHOG000055250.
InParanoidiP0AEX9.
KOiK10108.
OMAiWAWANID.
OrthoDBiEOG6CCH2B.
PhylomeDBiP0AEX9.

Family and domain databases

InterProiIPR006060. Maltose-bd.
IPR006061. SBP_1_CS.
IPR006059. SBP_1_dom.
[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

        10         20         30         40         50
MKIKTGARIL ALSALTTMMF SASALAKIEE GKLVIWINGD KGYNGLAEVG
60 70 80 90 100
KKFEKDTGIK VTVEHPDKLE EKFPQVAATG DGPDIIFWAH DRFGGYAQSG
110 120 130 140 150
LLAEITPDKA FQDKLYPFTW DAVRYNGKLI AYPIAVEALS LIYNKDLLPN
160 170 180 190 200
PPKTWEEIPA LDKELKAKGK SALMFNLQEP YFTWPLIAAD GGYAFKYENG
210 220 230 240 250
KYDIKDVGVD NAGAKAGLTF LVDLIKNKHM NADTDYSIAE AAFNKGETAM
260 270 280 290 300
TINGPWAWSN IDTSKVNYGV TVLPTFKGQP SKPFVGVLSA GINAASPNKE
310 320 330 340 350
LAKEFLENYL LTDEGLEAVN KDKPLGAVAL KSYEEELAKD PRIAATMENA
360 370 380 390
QKGEIMPNIP QMSAFWYAVR TAVINAASGR QTVDEALKDA QTRITK
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
2MV0NMR-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[»]
4JKMX-ray2.26C/D27-392[»]
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[»]
4N4XX-ray2.50A27-387[»]
4NDZX-ray3.45A/B/C/D/E/F27-393[»]
4R0YX-ray2.00A/B27-387[»]
4WJVX-ray3.20E/F/G/H27-393[»]
ProteinModelPortaliP0AEX9.
SMRiP0AEX9. Positions 27-392.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi852832. 1 interaction.
DIPiDIP-31871N.
IntActiP0AEX9. 10 interactions.
STRINGi511145.b4034.

Protein family/group databases

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

2D gel databases

SWISS-2DPAGEP0AEX9.

Proteomic databases

PaxDbiP0AEX9.
PRIDEiP0AEX9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EchoBASEiEB0549.
EcoGeneiEG10554. malE.

Phylogenomic databases

eggNOGiCOG2182.
HOGENOMiHOG000055250.
InParanoidiP0AEX9.
KOiK10108.
OMAiWAWANID.
OrthoDBiEOG6CCH2B.
PhylomeDBiP0AEX9.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP0AEX9.
PROiP0AEX9.

Gene expression databases

GenevestigatoriP0AEX9.

Family and domain databases

InterProiIPR006060. Maltose-bd.
IPR006061. SBP_1_CS.
IPR006059. SBP_1_dom.
[Graphical view]
PfamiPF01547. SBP_bac_1. 1 hit.
[Graphical view]
PRINTSiPR00181. MALTOSEBP.
PROSITEiPS01037. SBP_BACTERIAL_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: February 4, 2015
This is version 102 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.