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3.A.1.2.2
Arabinose porter (Horazdovsky and Hogg 1989).

Accession Number:P02924
Protein Name:AraF aka B1901
Length:329
Molecular Weight:35541.00
Species:Escherichia coli [83333]
Number of TMSs:1
Location1 / Topology2 / Orientation3: Periplasm1
Substrate Arabinose

Cross database links:

Genevestigator: P02924
EchoBASE: EB0055
EcoGene: EG10057
eggNOG: COG1879
HEGENOM: HBG298457
RefSeq: AP_002519.1    NP_416414.1   
Entrez Gene ID: 946409   
Pfam: PF00532   
Drugbank: Drugbank Link   
BioCyc: EcoCyc:ARAF-MONOMER    ECOL168927:B1901-MONOMER   
KEGG: ecj:JW1889    eco:b1901   

Gene Ontology

GO:0042597 C:periplasmic space
GO:0008643 P:carbohydrate transport

References (10)

[1] “High-affinity L-arabinose transport operon. Nucleotide sequence and analysis of gene products.”  Scripture J.B.et.al.   2445996
[2] “A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map.”  Itoh T.et.al.   9097040
[3] “The complete genome sequence of Escherichia coli K-12.”  Blattner F.R.et.al.   9278503
[4] “Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.”  Hayashi K.et.al.   16738553
[5] “The nucleotide sequences defining the signal peptides of the galactose-binding protein and the arabinose-binding protein.”  Scripture J.B.et.al.   6885805
[6] “Amino acid sequence of the L-arabinose-binding protein from Escherichia coli B/r.”  Hogg R.W.et.al.   326784
[7] “Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.”  Link A.J.et.al.   9298646
[8] “L-arabinose-binding protein-sugar complex at 2.4-A resolution. Stereochemistry and evidence for a structural change.”  Newcomer M.E.et.al.   7031057
[9] “The 2.8-A resolution structure of the L-arabinose-binding protein from Escherichia coli. Polypeptide chain folding, domain similarity, and probable location of sugar-binding site.”  Quiocho F.A.et.al.   326785
[10] “A Pro to Gly mutation in the hinge of the arabinose-binding protein enhances binding and alters specificity. Sugar-binding and crystallographic studies.”  Vermersch P.S.et.al.   2204627
Structure:
1ABE   1ABF   1APB   1BAP   2WRZ   5ABP   6ABP   7ABP   8ABP   9ABP   [...more]

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MHKFTKALAA IGLAAVMSQS AMAENLKLGF LVKQPEEPWF QTEWKFADKA GKDLGFEVIK 
61:	IAVPDGEKTL NAIDSLAASG AKGFVICTPD PKLGSAIVAK ARGYDMKVIA VDDQFVNAKG 
121:	KPMDTVPLVM MAATKIGERQ GQELYKEMQK RGWDVKESAV MAITANELDT ARRRTTGSMD 
181:	ALKAAGFPEK QIYQVPTKSN DIPGAFDAAN SMLVQHPEVK HWLIVGMNDS TVLGGVRATE 
241:	GQGFKAADII GIGINGVDAV SELSKAQATG FYGSLLPSPD VHGYKSSEML YNWVAKDVEP 
301:	PKFTEVTDVV LITRDNFKEE LEKKGLGGK