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show all sequences of 2.1.1.294

Coordination of polymerization, chain termination, and export in assembly of the Escherichia coli lipopolysaccharide O9a antigen in an ATP-binding cassette transporter-dependent pathway

Clarke, B.R.; Greenfield, L.K.; Bouwman, C.; Whitfield, C.; J. Biol. Chem. 284, 30662-30672 (2009)

Data extracted from this reference:

Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
the WbdD protein is tethered to the membrane via a C-terminal region containing amphipathic helices located between residues 601 and 669
Escherichia coli
16020
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
-
-
-
Escherichia coli O9a
-
-
-
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
the WbdD protein is tethered to the membrane via a C-terminal region containing amphipathic helices located between residues 601 and 669
Escherichia coli
16020
-
General Information
General Information
Commentary
Organism
malfunction
membrane preparations from a wbdD mutant have severely diminished mannosyltransferase activity in vitro, and no significant amounts of the WbdA protein are targeted to the membrane fraction. Expression of a polypeptide comprising the WbdD C-terminal region is sufficient to restore both proper localization of WbdA and mannosyltransferase activity
Escherichia coli
physiological function
WbdD controls polymerization reaction in biosynthesis of the O-polysaccharide by coordinating the correct membrane association required for activity of one of the critical mannosyltransferases, WbdA. Identification of regions in the C terminus of WbdD that contribute to the interaction
Escherichia coli
General Information (protein specific)
General Information
Commentary
Organism
malfunction
membrane preparations from a wbdD mutant have severely diminished mannosyltransferase activity in vitro, and no significant amounts of the WbdA protein are targeted to the membrane fraction. Expression of a polypeptide comprising the WbdD C-terminal region is sufficient to restore both proper localization of WbdA and mannosyltransferase activity
Escherichia coli
physiological function
WbdD controls polymerization reaction in biosynthesis of the O-polysaccharide by coordinating the correct membrane association required for activity of one of the critical mannosyltransferases, WbdA. Identification of regions in the C terminus of WbdD that contribute to the interaction
Escherichia coli
Other publictions for EC 2.1.1.294
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
736468
Liston
Domain interactions control co ...
Escherichia coli
J. Biol. Chem.
290
1075-1085
2015
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1
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2
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2
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2
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1
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2
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1
1
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722733
Clarke
In vitro reconstruction of the ...
Escherichia coli, Escherichia coli O9a
J. Biol. Chem.
286
41391-41401
2011
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1
2
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4
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4
1
1
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1
1
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722664
Clarke
Coordination of polymerization ...
Escherichia coli, Escherichia coli O9a
J. Biol. Chem.
284
30662-30672
2009
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1
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6
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2
2
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722640
Clarke
Nonreducing terminal modificat ...
Escherichia coli, Escherichia coli O9a
J. Biol. Chem.
279
35709-35718
2004
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1
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4
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1
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