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Protein

Maltose-binding periplasmic protein

Gene

malE

Organism
Escherichia coli O157:H7
Status
Reviewed-Annotation score: Annotation score: 2 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 (By similarity).By similarity

GO - Molecular functioni

  1. maltose transmembrane transporter activity Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Sugar transport, Transport

Enzyme and pathway databases

BioCyciECOL386585:GJFA-5020-MONOMER.
ECOO157:MALE-MONOMER.

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:Z5632, ECs5017
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000558 Componenti: Chromosome UP000002519 Componenti: Chromosome

Subcellular locationi

  1. Periplasm By similarity

GO - Cellular componenti

  1. periplasmic space Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626By similarityAdd
BLAST
Chaini27 – 396370Maltose-binding periplasmic proteinPRO_0000044622Add
BLAST

Proteomic databases

PRIDEiP0AEY0.

Interactioni

Protein-protein interaction databases

IntActiP0AEY0. 1 interaction.
MINTiMINT-6765486.
STRINGi155864.Z5632.

Structurei

Secondary structure

1
396
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi33 – 364Combined sources
Helixi43 – 5715Combined sources
Beta strandi61 – 644Combined sources
Helixi69 – 779Combined sources
Turni78 – 803Combined sources
Beta strandi84 – 896Combined sources
Helixi90 – 923Combined sources
Helixi93 – 986Combined sources
Helixi109 – 1124Combined sources
Helixi117 – 1226Combined sources
Beta strandi131 – 1377Combined sources
Beta strandi140 – 1445Combined sources
Turni145 – 1473Combined sources
Helixi155 – 1573Combined sources
Helixi158 – 1669Combined sources
Turni167 – 1693Combined sources
Beta strandi171 – 1733Combined sources
Beta strandi177 – 1793Combined sources
Helixi180 – 1823Combined sources
Helixi184 – 1896Combined sources
Beta strandi193 – 1953Combined sources
Beta strandi207 – 2115Combined sources
Helixi212 – 22615Combined sources
Helixi236 – 2449Combined sources
Beta strandi247 – 2537Combined sources
Helixi255 – 2573Combined sources
Helixi258 – 2647Combined sources
Beta strandi268 – 2714Combined sources
Beta strandi284 – 29310Combined sources
Helixi299 – 30810Combined sources
Helixi313 – 3208Combined sources
Beta strandi327 – 3304Combined sources
Helixi331 – 3377Combined sources
Helixi341 – 35212Combined sources
Beta strandi353 – 3553Combined sources
Helixi362 – 37716Combined sources
Beta strandi378 – 3814Combined sources
Helixi383 – 39210Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3VD8X-ray2.07A27-384[»]
4MY2X-ray2.40A26-392[»]
4WGIX-ray1.85A27-392[»]
4XAIX-ray2.60A/B27-392[»]
4XAJX-ray3.55A/B/C/D26-392[»]
ProteinModelPortaliP0AEY0.
SMRiP0AEY0. Positions 27-392.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2182.
HOGENOMiHOG000055250.
KOiK10108.
OMAiWAWANID.
OrthoDBiEOG6CCH2B.

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.

P0AEY0-1 [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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG59233.1.
BA000007 Genomic DNA. Translation: BAB38440.1.
PIRiA98256.
E86096.
RefSeqiNP_290668.1. NC_002655.2.
NP_313044.1. NC_002695.1.

Genome annotation databases

EnsemblBacteriaiAAG59233; AAG59233; Z5632.
BAB38440; BAB38440; BAB38440.
GeneIDi914317.
960089.
KEGGiece:Z5632.
ecs:ECs5017.
PATRICi18359629. VBIEscCol44059_4951.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG59233.1.
BA000007 Genomic DNA. Translation: BAB38440.1.
PIRiA98256.
E86096.
RefSeqiNP_290668.1. NC_002655.2.
NP_313044.1. NC_002695.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3VD8X-ray2.07A27-384[»]
4MY2X-ray2.40A26-392[»]
4WGIX-ray1.85A27-392[»]
4XAIX-ray2.60A/B27-392[»]
4XAJX-ray3.55A/B/C/D26-392[»]
ProteinModelPortaliP0AEY0.
SMRiP0AEY0. Positions 27-392.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP0AEY0. 1 interaction.
MINTiMINT-6765486.
STRINGi155864.Z5632.

Proteomic databases

PRIDEiP0AEY0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG59233; AAG59233; Z5632.
BAB38440; BAB38440; BAB38440.
GeneIDi914317.
960089.
KEGGiece:Z5632.
ecs:ECs5017.
PATRICi18359629. VBIEscCol44059_4951.

Phylogenomic databases

eggNOGiCOG2182.
HOGENOMiHOG000055250.
KOiK10108.
OMAiWAWANID.
OrthoDBiEOG6CCH2B.

Enzyme and pathway databases

BioCyciECOL386585:GJFA-5020-MONOMER.
ECOO157:MALE-MONOMER.

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

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
  2. "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
    Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.
    , Kuhara S., Shiba T., Hattori M., Shinagawa H.
    DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Entry informationi

Entry nameiMALE_ECO57
AccessioniPrimary (citable) accession number: P0AEY0
Secondary accession number(s): P02928
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 29, 2015
This is version 68 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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.