Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein
Submitted name:

Mmbp

Gene

malE

Organism
Escherichia coli (strain MS 21-1)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Submitted name:
MmbpImported
Gene namesi
Name:malEImported
ORF Names:HMPREF9530_03068Imported
OrganismiEscherichia coli (strain MS 21-1)Imported
Taxonomic identifieri749527 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XZ3X-ray1.95A27-392[»]
3OB4X-ray2.71A27-393[»]
4H1GX-ray2.15A27-387[»]
4TSMX-ray1.90A/B/C27-392[»]
ProteinModelPortaliD8A942.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

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.

D8A942-1 [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 QTVDAALKDA QTRITK
Length:396
Mass (Da):43,330
Last modified:October 5, 2010 - v1
Checksum:iA4C1B3C4637ADE47
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
ADTR01000284 Genomic DNA. Translation: EFK20320.1.
RefSeqiWP_000695386.1. NZ_GG772719.1.

Genome annotation databases

EnsemblBacteriaiEFK20320; EFK20320; HMPREF9530_03068.
PATRICi41830752. VBIEscCol155740_2888.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
ADTR01000284 Genomic DNA. Translation: EFK20320.1.
RefSeqiWP_000695386.1. NZ_GG772719.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XZ3X-ray1.95A27-392[»]
3OB4X-ray2.71A27-393[»]
4H1GX-ray2.15A27-387[»]
4TSMX-ray1.90A/B/C27-392[»]
ProteinModelPortaliD8A942.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiEFK20320; EFK20320; HMPREF9530_03068.
PATRICi41830752. VBIEscCol155740_2888.

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.
    Strain: MS 21-1Imported.
  2. "Crystal Structure of MBP-fusion allergen."
    Mueller G.A., Gosavi R.A., Moon A.F., London R.E., Pedersen L.C.
    Submitted (AUG-2010) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) OF 27-393.
  3. "Charge-surrounded pockets and electrostatic interactions with small ions modulate the activity of retroviral fusion proteins."
    Lamb D., Schuttelkopf A.W., van Aalten D.M., Brighty D.W.
    PLoS Pathog. 7:e1001268-e1001268(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 27-392.
  4. "Crystal structure of the Candida albicans Kar3 kinesin motor domain fused to maltose-binding protein."
    Delorme C., Joshi M., Allingham J.S.
    Biochem. Biophys. Res. Commun. 428:427-432(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 27-387.
  5. "Structural and evolutionary analyses show unique stabilization strategies in the type IV pili of Clostridium difficile."
    Piepenbrink K.H., Maldarelli G.A., Martinez de la Pena C.F., Dingle T.C., Mulvey G.L., Lee A., von Rosenvinge E., Armstrong G.D., Donnenberg M.S., Sundberg E.J.
    Structure 23:385-396(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 27-392.

Entry informationi

Entry nameiD8A942_ECOMS
AccessioniPrimary (citable) accession number: D8A942
Entry historyi
Integrated into UniProtKB/TrEMBL: October 5, 2010
Last sequence update: October 5, 2010
Last modified: May 27, 2015
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.Imported

Keywords - Technical termi

3D-structureCombined sources

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.