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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

  • maltose binding Source: EcoCyc
  • maltose transmembrane transporter activity Source: InterPro
  • transporter activity Source: EcoliWiki

GO - Biological processi

  • carbohydrate transport Source: EcoliWiki
  • cell chemotaxis Source: EcoCyc
  • cellular response to DNA damage stimulus Source: EcoliWiki
  • detection of maltose stimulus Source: EcoCyc
  • maltodextrin transport Source: EcoCyc
  • maltose transport Source: EcoCyc
  • 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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10554. malE.

Subcellular locationi

GO - Cellular componenti

  • ATP-binding cassette (ABC) transporter complex Source: EcoliWiki
  • ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing Source: EcoCyc
  • maltose transport complex Source: EcoCyc
  • outer membrane-bounded periplasmic space Source: EcoCyc
  • periplasmic space Source: EcoliWiki
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 262 PublicationsAdd BLAST26
ChainiPRO_000003169427 – 396Maltose-binding periplasmic proteinAdd BLAST370

Proteomic databases

PaxDbiP0AEX9.
PRIDEiP0AEX9.

2D gel databases

SWISS-2DPAGEP0AEX9.

Expressioni

Inductioni

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

Interactioni

Binary interactionsi

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

Protein-protein interaction databases

BioGridi4263065. 9 interactors.
852832. 1 interactor.
DIPiDIP-31871N.
IntActiP0AEX9. 10 interactors.
STRINGi511145.b4034.

Structurei

Secondary structure

1396
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni28 – 31Combined sources4
Beta strandi32 – 36Combined sources5
Helixi39 – 41Combined sources3
Helixi43 – 57Combined sources15
Beta strandi60 – 64Combined sources5
Helixi69 – 76Combined sources8
Turni77 – 80Combined sources4
Beta strandi84 – 89Combined sources6
Helixi90 – 92Combined sources3
Helixi93 – 98Combined sources6
Beta strandi99 – 101Combined sources3
Helixi109 – 112Combined sources4
Helixi117 – 122Combined sources6
Beta strandi123 – 125Combined sources3
Beta strandi126 – 129Combined sources4
Beta strandi131 – 137Combined sources7
Beta strandi140 – 144Combined sources5
Turni145 – 147Combined sources3
Beta strandi148 – 150Combined sources3
Beta strandi153 – 155Combined sources3
Helixi158 – 166Combined sources9
Turni167 – 169Combined sources3
Beta strandi171 – 173Combined sources3
Beta strandi177 – 179Combined sources3
Helixi180 – 189Combined sources10
Beta strandi193 – 198Combined sources6
Beta strandi201 – 208Combined sources8
Beta strandi209 – 211Combined sources3
Helixi212 – 226Combined sources15
Beta strandi227 – 230Combined sources4
Helixi236 – 244Combined sources9
Beta strandi248 – 253Combined sources6
Helixi255 – 257Combined sources3
Helixi258 – 263Combined sources6
Beta strandi264 – 266Combined sources3
Beta strandi268 – 271Combined sources4
Beta strandi275 – 279Combined sources5
Beta strandi284 – 293Combined sources10
Beta strandi294 – 297Combined sources4
Helixi299 – 308Combined sources10
Turni309 – 311Combined sources3
Helixi313 – 322Combined sources10
Beta strandi323 – 325Combined sources3
Beta strandi327 – 330Combined sources4
Helixi331 – 337Combined sources7
Beta strandi338 – 340Combined sources3
Helixi341 – 352Combined sources12
Beta strandi353 – 355Combined sources3
Helixi362 – 377Combined sources16
Beta strandi379 – 381Combined sources3
Helixi383 – 392Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
2N44NMR-A27-396[»]
2N45NMR-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[»]
3D4CX-ray2.90A27-393[»]
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/C27-392[»]
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[»]
3J9Pelectron microscopy4.24A/B/C/D27-392[»]
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[»]
3WOAX-ray2.00A27-393[»]
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[»]
4LOGX-ray2.70A/B26-392[»]
4MBPX-ray1.70A27-396[»]
4N4XX-ray2.50A27-387[»]
4NDZX-ray3.45A/B/C/D/E/F27-393[»]
4O2XX-ray2.70A/B27-396[»]
4OGMX-ray2.23A27-387[»]
4PE2X-ray1.72A27-392[»]
4QSZX-ray2.86A/B27-387[»]
4QVHX-ray1.75A/B27-392[»]
4R0YX-ray2.00A/B27-387[»]
4RG5X-ray1.70A/B27-395[»]
4RWFX-ray1.76A26-392[»]
4RWGX-ray2.44A/B/C26-392[»]
4TSMX-ray1.90A/B/C27-392[»]
4WJVX-ray3.20E/F/G/H27-393[»]
4WMSX-ray1.90A27-392[»]
4WMTX-ray2.35A27-392[»]
4WMUX-ray1.55A27-392[»]
4WMVX-ray2.40A27-392[»]
4WMWX-ray1.90A27-392[»]
4WMXX-ray2.00A27-392[»]
4WRNX-ray3.20A/B27-393[»]
4WTHX-ray2.25A/B27-392[»]
4WVHX-ray2.10A33-392[»]
4XA2X-ray1.98A/B27-392[»]
4XHSX-ray1.70A/B27-392[»]
4XR8X-ray2.25A/B27-392[»]
4XZSX-ray2.12A/B27-392[»]
4XZVX-ray3.58A/C/E/G27-392[»]
5AQ9X-ray1.86B/D33-392[»]
5AZ6X-ray2.56A/B27-394[»]
5AZ7X-ray1.96A27-394[»]
5AZ8X-ray1.70A27-394[»]
5AZ9X-ray1.82A27-394[»]
5AZAX-ray2.08A27-394[»]
5C7RX-ray1.94A/B27-384[»]
5CBNX-ray2.30B27-392[»]
5CFVX-ray1.80A27-392[»]
5DFMX-ray2.30A/B27-384[»]
5DISX-ray2.85D32-387[»]
5E24X-ray2.14A/C27-396[»]
5EDUX-ray2.79A/B27-392[»]
5FSGX-ray3.21A27-384[»]
5GRUX-ray1.96A27-392[»]
5GS2X-ray3.59A27-393[»]
5HZ7X-ray1.43A27-392[»]
5I69X-ray2.70A27-392[»]
5IHJX-ray2.20A27-392[»]
5IQZX-ray2.33A27-392[»]
5JJ4X-ray2.81A/B/C27-393[»]
5JTQNMR-E/F108-149[»]
5JTRNMR-E/F/G/H168-207[»]
5LDFelectron microscopy6.20M/N/O/P/Q/R/S/T/U/V/W/X27-396[»]
ProteinModelPortaliP0AEX9.
SMRiP0AEX9.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AEX9.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4107FKK. Bacteria.
COG2182. LUCA.
HOGENOMiHOG000055250.
InParanoidiP0AEX9.
KOiK10108.
OMAiWAWANID.
PhylomeDBiP0AEX9.

Family and domain databases

InterProiIPR006060. Maltose-bd.
IPR006061. SBP_1_CS.
[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)DescriptionActionsGraphical viewLength
Sequence conflicti36W → A AA sequence (PubMed:9298646).Curated1
Sequence conflicti46L → H in CAA23581 (PubMed:6283312).Curated1

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.
WP_000695387.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77004; AAC77004; b4034.
BAE78036; BAE78036; BAE78036.
GeneIDi948538.
KEGGiecj:JW3994.
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.
WP_000695387.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
2N44NMR-A27-396[»]
2N45NMR-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[»]
3D4CX-ray2.90A27-393[»]
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/C27-392[»]
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[»]
3J9Pelectron microscopy4.24A/B/C/D27-392[»]
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[»]
3WOAX-ray2.00A27-393[»]
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[»]
4LOGX-ray2.70A/B26-392[»]
4MBPX-ray1.70A27-396[»]
4N4XX-ray2.50A27-387[»]
4NDZX-ray3.45A/B/C/D/E/F27-393[»]
4O2XX-ray2.70A/B27-396[»]
4OGMX-ray2.23A27-387[»]
4PE2X-ray1.72A27-392[»]
4QSZX-ray2.86A/B27-387[»]
4QVHX-ray1.75A/B27-392[»]
4R0YX-ray2.00A/B27-387[»]
4RG5X-ray1.70A/B27-395[»]
4RWFX-ray1.76A26-392[»]
4RWGX-ray2.44A/B/C26-392[»]
4TSMX-ray1.90A/B/C27-392[»]
4WJVX-ray3.20E/F/G/H27-393[»]
4WMSX-ray1.90A27-392[»]
4WMTX-ray2.35A27-392[»]
4WMUX-ray1.55A27-392[»]
4WMVX-ray2.40A27-392[»]
4WMWX-ray1.90A27-392[»]
4WMXX-ray2.00A27-392[»]
4WRNX-ray3.20A/B27-393[»]
4WTHX-ray2.25A/B27-392[»]
4WVHX-ray2.10A33-392[»]
4XA2X-ray1.98A/B27-392[»]
4XHSX-ray1.70A/B27-392[»]
4XR8X-ray2.25A/B27-392[»]
4XZSX-ray2.12A/B27-392[»]
4XZVX-ray3.58A/C/E/G27-392[»]
5AQ9X-ray1.86B/D33-392[»]
5AZ6X-ray2.56A/B27-394[»]
5AZ7X-ray1.96A27-394[»]
5AZ8X-ray1.70A27-394[»]
5AZ9X-ray1.82A27-394[»]
5AZAX-ray2.08A27-394[»]
5C7RX-ray1.94A/B27-384[»]
5CBNX-ray2.30B27-392[»]
5CFVX-ray1.80A27-392[»]
5DFMX-ray2.30A/B27-384[»]
5DISX-ray2.85D32-387[»]
5E24X-ray2.14A/C27-396[»]
5EDUX-ray2.79A/B27-392[»]
5FSGX-ray3.21A27-384[»]
5GRUX-ray1.96A27-392[»]
5GS2X-ray3.59A27-393[»]
5HZ7X-ray1.43A27-392[»]
5I69X-ray2.70A27-392[»]
5IHJX-ray2.20A27-392[»]
5IQZX-ray2.33A27-392[»]
5JJ4X-ray2.81A/B/C27-393[»]
5JTQNMR-E/F108-149[»]
5JTRNMR-E/F/G/H168-207[»]
5LDFelectron microscopy6.20M/N/O/P/Q/R/S/T/U/V/W/X27-396[»]
ProteinModelPortaliP0AEX9.
SMRiP0AEX9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263065. 9 interactors.
852832. 1 interactor.
DIPiDIP-31871N.
IntActiP0AEX9. 10 interactors.
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.
GeneIDi948538.
KEGGiecj:JW3994.
eco:b4034.
PATRICi32123601. VBIEscCol129921_4149.

Organism-specific databases

EchoBASEiEB0549.
EcoGeneiEG10554. malE.

Phylogenomic databases

eggNOGiENOG4107FKK. Bacteria.
COG2182. LUCA.
HOGENOMiHOG000055250.
InParanoidiP0AEX9.
KOiK10108.
OMAiWAWANID.
PhylomeDBiP0AEX9.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP0AEX9.
PROiP0AEX9.

Family and domain databases

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

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: November 30, 2016
This is version 121 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

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 one 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.