TCDB is operated by the Saier Lab Bioinformatics Group
« See all members of the family


3.A.1.2.6
D-allose porter.  The structure of AlsB has been solved at 1.8 Å resolution (Chaudhuri et al. 1999). Ten residues from both the domains form 14 hydrogen bonds with the sugar. 6-Deoxy-allose, 3-deoxy-glucose and ribose bind with reduced affinity so AlbP can function as a low affinity transporter for D-ribose (Chaudhuri et al. 1999).

Accession Number:P39265
Protein Name:AlsB aka B4088
Length:311
Molecular Weight:32910.00
Species:Escherichia coli [83333]
Number of TMSs:1
Location1 / Topology2 / Orientation3: Periplasm1
Substrate allose

Cross database links:

RefSeq: AP_004590.1    NP_418512.1   
Entrez Gene ID: 948604   
Pfam: PF00532   
BioCyc: EcoCyc:YJCX-MONOMER    ECOL168927:B4088-MONOMER   
KEGG: ecj:JW4049    eco:b4088   

Gene Ontology

GO:0016020 C:membrane
GO:0042597 C:periplasmic space
GO:0008643 P:carbohydrate transport

References (6)

[1] “Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes.”  Burland V.D.et.al.   7610040
[2] “The complete genome sequence of Escherichia coli K-12.”  Blattner F.R.et.al.   9278503
[3] “Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.”  Hayashi K.et.al.   16738553
[4] “Ribose catabolism of Escherichia coli: characterization of the rpiB gene encoding ribose phosphate isomerase B and of the rpiR gene, which is involved in regulation of rpiB expression.”  Soerensen K.I.et.al.   8576032
[5] “The D-allose operon of Escherichia coli K-12.”  Kim C.et.al.   9401019
[6] “Structure of D-allose binding protein from Escherichia coli bound to D-allose at 1.8-A resolution.”  Chaudhuri B.N.et.al.   10064713
Structure:
1GUB   1GUD   1RPJ     

External Searches:

Analyze:

Predict TMSs (Predict number of transmembrane segments)
Window Size: Angle:  
FASTA formatted sequence
1:	MNKYLKYFSG TLVGLMLSTS AFAAAEYAVV LKTLSNPFWV DMKKGIEDEA KTLGVSVDIF 
61:	ASPSEGDFQS QLQLFEDLSN KNYKGIAFAP LSSVNLVMPV ARAWKKGIYL VNLDEKIDMD 
121:	NLKKAGGNVE AFVTTDNVAV GAKGASFIID KLGAEGGEVA IIEGKAGNAS GEARRNGATE 
181:	AFKKASQIKL VASQPADWDR IKALDVATNV LQRNPNIKAI YCANDTMAMG VAQAVANAGK 
241:	TGKVLVVGTD GIPEARKMVE AGQMTATVAQ NPADIGATGL KLMVDAEKSG KVIPLDKAPE 
301:	FKLVDSILVT Q