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InterPro: IPR003501 Phosphotransferase system, lactose/cellobiose-specific IIB subunit

Protein matchesHelp
UniProtKB
Matches:
3575 proteins
AccessionHelp IPR003501 PTS_IIB_lac
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Children IPR013012 Phosphotransferase system, EIIB component, type 3
Found in IPR017180 Phosphotransferase system component IIBC, sugar-specific, predicted
Contains IPR013011 Phosphotransferase system, EIIB component, type 2
GO Term annotationHelp
Process GO:0009401 phosphoenolpyruvate-dependent sugar phosphotransferase system
Function GO:0005351 sugar:hydrogen symporter activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

The bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS) is a multi-protein system involved in the regulation of a variety of metabolic and transcriptional processes. The lactose/cellobiose-specific family are one of four structurally and functionally distinct group IIB PTS system cytoplasmic enzymes. The fold of IIB cellobiose shows similar structure to mammalian tyrosine phosphatases. This signature is often found downstream of IPR003352.

Structural linksHelp
SCOP: c.44.2.1
Database linksHelp
Enzyme: EC:2.7.1.69
PANDIT: PF02302
Blocks: IPB003501

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR003501 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P00550 PTS system mannitol-specific EIICBA component

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR003501 Phosphotransferase system, lactose/cellobiose-specific IIB subunit
IPR003352 Phosphotransferase system, EIIC
IPR002178 Phosphotransferase system, phosphoenolpyruvate-dependent sugar EIIA 2
IPR004718 Phosphotransferase system, mannitol-specific enzyme IIC
IPR016152 Phosphotransferase/anion transporter
IPR013014 Phosphotransferase system, EIIC component, type 2
IPR013011 Phosphotransferase system, EIIB component, type 2
PDB Chain
ModBase
CATH Domain
SCOP Domain

PublicationsHelp

Additional ReadingHelp
Legler PM, Cai M, Peterkofsky A, Clore GM.
Three-dimensional solution structure of the cytoplasmic B domain of the mannitol transporter IImannitol of the Escherichia coli phosphotransferase system.
J. Biol. Chem. 279 2004 39115-21 [PubMed: 15258141]
http://dx.doi.org/10.1074/jbc.M406764200
Ab E, Schuurman-Wolters GK, Nijlant D, Dijkstra K, Saier MH, Robillard GT, Scheek RM.
NMR structure of cysteinyl-phosphorylated enzyme IIB of the N,N'-diacetylchitobiose-specific phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli.
J. Mol. Biol. 308 2001 993-1009 [PubMed: 11352587]
http://dx.doi.org/10.1006/jmbi.2001.4623
Suh JY, Tang C, Cai M, Clore GM.
Visualization of the phosphorylated active site loop of the cytoplasmic B domain of the mannitol transporter II(Mannitol) of the Escherichia coli phosphotransferase system by NMR spectroscopy and residual dipolar couplings.
J. Mol. Biol. 353 2005 1129-36 [PubMed: 16219324]
http://dx.doi.org/10.1016/j.jmb.2005.09.033
Suh JY, Cai M, Williams DC Jr, Clore GM.
Solution structure of a post-transition state analog of the phosphotransfer reaction between the A and B cytoplasmic domains of the mannitol transporter IIMannitol of the Escherichia coli phosphotransferase system.
J. Biol. Chem. 281 2006 8939-49 [PubMed: 16443929]
http://dx.doi.org/10.1074/jbc.M513466200
Ab E, Schuurman-Wolters G, Reizer J, Saier MH, Dijkstra K, Scheek RM, Robillard GT.
The NMR side-chain assignments and solution structure of enzyme IIBcellobiose of the phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli.
Protein Sci. 6 1997 304-14 [PubMed: 9041631]
http://www.proteinscience.org/cgi/content/abstract/6/2/304
van Montfort RL, Pijning T, Kalk KH, Reizer J, Saier MH Jr, Thunnissen MM, Robillard GT, Dijkstra BW.
The structure of an energy-coupling protein from bacteria, IIBcellobiose, reveals similarity to eukaryotic protein tyrosine phosphatases.
Structure 5 1997 217-25 [PubMed: 9032081]
http://dx.doi.org/10.1016/S0969-2126(97)00180-9
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InterPro 23.1