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4.A.3.2.1
N,N'-diacetylchitobiose (Chb) porter (also transports cellobiose; Kachroo et al., 2007).

Accession Number:P69795
Protein Name:PTCB aka ChbB aka CELA aka B1738
Length:106
Molecular Weight:11427.00
Species:Escherichia coli [83333]
Location1 / Topology2 / Orientation3: Cytoplasm1
Substrate cellobiose, N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-aldehydo-D-glucosamine

Cross database links:

RefSeq: AP_002357.1    NP_416252.1   
Entrez Gene ID: 945339   
Pfam: PF02302   
BioCyc: EcoCyc:CELA-MONOMER    ECOL168927:B1738-MONOMER   
KEGG: ecj:JW1727    eco:b1738   

Gene Ontology

GO:0005737 C:cytoplasm
GO:0016301 F:kinase activity
GO:0008982 F:protein-N(PI)-phosphohistidine-sugar phosph...
GO:0005529 F:sugar binding
GO:0009401 P:phosphoenolpyruvate-dependent sugar phospho...

References (12)

[1] “Characterization and nucleotide sequence of the cryptic cel operon of Escherichia coli K12.”  Parker L.L.et.al.   2179047
[2] “A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map.”  Aiba H.et.al.   9097039
[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 cellobiose permease of Escherichia coli consists of three proteins and is homologous to the lactose permease of Staphylococcus aureus.”  Reizer J.et.al.   2092358
[6] “Wild-type Escherichia coli grows on the chitin disaccharide, N,N'-diacetylchitobiose, by expressing the cel operon.”  Keyhani N.O.et.al.   9405618
[7] “The chitin disaccharide, N,N'-diacetylchitobiose, is catabolized by Escherichia coli and is transported/phosphorylated by the phosphoenolpyruvate:glycose phosphotransferase system.”  Keyhani N.O.et.al.   10913117
[8] “The transport/phosphorylation of N,N'-diacetylchitobiose in Escherichia coli. Characterization of phospho-IIB(Chb) and of a potential transition state analogue in the phosphotransfer reaction between the proteins IIA(Chb) and IIB(Chb).”  Keyhani N.O.et.al.   10913119
[9] “Analytical sedimentation of the IIAChb and IIBChb proteins of the Escherichia coli N,N'-diacetylchitobiose phosphotransferase system. Demonstration of a model phosphotransfer transition state complex.”  Keyhani N.O.et.al.   10913122
[10] “Enzyme IIBcellobiose of the phosphoenol-pyruvate-dependent phosphotransferase system of Escherichia coli: backbone assignment and secondary structure determined by three-dimensional NMR spectroscopy.”  Ab E.et.al.   8003964
[11] “The NMR side-chain assignments and solution structure of enzyme IIBcellobiose of the phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli.”  Ab E.et.al.   9041631
[12] “The structure of an energy-coupling protein from bacteria, IIBcellobiose, reveals similarity to eukaryotic protein tyrosine phosphatases.”  van Montfort R.L.M.et.al.   9032081
Structure:
1E2B   1H9C   1IIB   2WWV   2WY2     

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MEKKHIYLFC SAGMSTSLLV SKMRAQAEKY EVPVIIEAFP ETLAGEKGQN ADVVLLGPQI 
61:	AYMLPEIQRL LPNKPVEVID SLLYGKVDGL GVLKAAVAAI KKAAAN