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3.A.1.2.1
Ribose porter.  RbsA has two ATPase domains fused together; RbsB is the substrate receptor; RbsC has 10 TMSs with N- and C-termini in the cytoplasm and forms a dimer (Stewart and Hermodson, 2003).  ABC importers can be divided into two classes. Type I importers follow an alternating access mechanism driven by the presence of the substrate. Type II importers accept substrates in a nucleotide-free state, with hydrolysis driving an inward-facing conformation.  RbsABC2 seems to share functional traits with both type I and type II importers, as well as possessing unique features, and employs a distinct mechanism relative to other ABC transporters (Clifton et al. 2014).

Accession Number:P02925
Protein Name:RbsB aka RBSP aka PRLB aka B3751
Length:296
Molecular Weight:30950.00
Species:Escherichia coli [83333]
Number of TMSs:1
Location1 / Topology2 / Orientation3: Periplasm1
Substrate Ribose

Cross database links:

DIP: DIP-10641N
RefSeq: AP_004036.1    NP_418207.1   
Entrez Gene ID: 948261   
Pfam: PF00532   
BioCyc: EcoCyc:RBSB-MONOMER    ECOL168927:B3751-MONOMER   
KEGG: ecj:JW3730    eco:b3751   

Gene Ontology

GO:0016020 C:membrane
GO:0042597 C:periplasmic space
GO:0008643 P:carbohydrate transport
GO:0006935 P:chemotaxis

References (11)

[1] “The amino acid sequence of D-ribose-binding protein from Escherichia coli K12.”  Groarke J.M.et.al.   6313683
[2] “DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication.”  Burland V.D.et.al.   7686882
[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 of the rbsD, rbsA, and rbsC genes of Escherichia coli K12.”  Bell A.W.et.al.   3011793
[6] “Ribokinase from Escherichia coli K12. Nucleotide sequence and overexpression of the rbsK gene and purification of ribokinase.”  Hope J.N.et.al.   3011794
[7] “FIS is a regulator of metabolism in Escherichia coli.”  Gonzalez-Gil G.et.al.   8899705
[8] “Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.”  Link A.J.et.al.   9298646
[9] “1.7-A X-ray structure of the periplasmic ribose receptor from Escherichia coli.”  Mowbray S.L.et.al.   1583688
[10] “Probing protein-protein interactions. The ribose-binding protein in bacterial transport and chemotaxis.”  Bjoerkman A.J.et.al.   7982928
[11] “Multiple open forms of ribose-binding protein trace the path of its conformational change.”  Bjoerkman A.J.et.al.   9641984
Structure:
1BA2   1DBP   1DRJ   1DRK   1URP   2DRI   2GX6     

External Searches:

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MNMKKLATLV SAVALSATVS ANAMAKDTIA LVVSTLNNPF FVSLKDGAQK EADKLGYNLV 
61:	VLDSQNNPAK ELANVQDLTV RGTKILLINP TDSDAVGNAV KMANQANIPV ITLDRQATKG 
121:	EVVSHIASDN VLGGKIAGDY IAKKAGEGAK VIELQGIAGT SAARERGEGF QQAVAAHKFN 
181:	VLASQPADFD RIKGLNVMQN LLTAHPDVQA VFAQNDEMAL GALRALQTAG KSDVMVVGFD 
241:	GTPDGEKAVN DGKLAATIAQ LPDQIGAKGV ETADKVLKGE KVQAKYPVDL KLVVKQ