BRENDA - Enzyme Database show
show all sequences of 2.1.1.294

Domain interactions control complex formation and polymerase specificity in the biosynthesis of the Escherichia coli O9a antigen

Liston, S.D.; Clarke, B.R.; Greenfield, L.K.; Richards, M.R.; Lowary, T.L.; Whitfield, C.; J. Biol. Chem. 290, 1075-1085 (2015)

Data extracted from this reference:

Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
peripheral membrane protein
Escherichia coli
16020
-
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Escherichia coli
enzyme WbdD is also active as polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol kinase, EC 2.7.1.181
?
-
-
-
S-adenosyl-L-methionine + O9a antigenic polysaccharide
Escherichia coli
-
S-adenosyl-L-homocysteine + methylated O9a antigenic polysaccharide
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
enzyme WbdD is also active as polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol kinase, EC 2.7.1.181
736468
Escherichia coli
?
-
-
-
-
S-adenosyl-L-methionine + O9a antigenic polysaccharide
-
736468
Escherichia coli
S-adenosyl-L-homocysteine + methylated O9a antigenic polysaccharide
-
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
S-adenosyl-L-methionine
-
Escherichia coli
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
S-adenosyl-L-methionine
-
Escherichia coli
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
peripheral membrane protein
Escherichia coli
16020
-
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Escherichia coli
enzyme WbdD is also active as polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol kinase, EC 2.7.1.181
?
-
-
-
S-adenosyl-L-methionine + O9a antigenic polysaccharide
Escherichia coli
-
S-adenosyl-L-homocysteine + methylated O9a antigenic polysaccharide
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
enzyme WbdD is also active as polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol kinase, EC 2.7.1.181
736468
Escherichia coli
?
-
-
-
-
S-adenosyl-L-methionine + O9a antigenic polysaccharide
-
736468
Escherichia coli
S-adenosyl-L-homocysteine + methylated O9a antigenic polysaccharide
-
-
-
?
General Information
General Information
Commentary
Organism
physiological function
In Escherichia coli O9a, the peripheral membrane protein WbdD terminates polymerization by adding a methyl phosphate to the non-reducing end of the nascent O9a polymer. The O9a system is a representative of the widespread ATP-binding cassette transporter-dependent assembly pathway. This terminal modification is required for recognition and export of the completed O-PS across the cytoplasmic membrane by its cognate ATP-binding cassette transporter. The recognition event is mediated by the nucleotide-binding domain polypeptide of the transporter, which possesses a serotype-specific carbohydrate-binding module that only binds terminated O-PS chains. The WbdD terminator plays an additional pivotal structural role in recruiting WbdA to the membrane. The stoichiometry of WbdA:WbdD in active complexes is a critical factor in establishing the chain length distribution of the resulting glycans. The size of the O9a polysaccharide is determined by the chain-terminating dual kinase/methyltransferase (WbdD) that is tethered to the membrane and recruits polymerase/glycosyltransferase WbdA into an active enzyme complex by protein-protein interactions. Identification via bacterial two-hybrid analysis of a surface-exposed alpha-helix in the C-terminal mannosyltransferase domain of WbdA as the site of interaction with WbdD, the C-terminal domain was unable to interact with WbdD in the absence of its N-terminal partner. The WbdD protein orchestrates critical localization and coordination of activities involved in chain extension and termination. Complex domain interactions are needed to position the polymerase components appropriately for assembly into a functional complex located at the cytoplasmic membrane. WbdD is therefore a central player in a sophisticated quality control system that dictates the distribution of chain lengths and marks those chains with a terminal export tag
Escherichia coli
General Information (protein specific)
General Information
Commentary
Organism
physiological function
In Escherichia coli O9a, the peripheral membrane protein WbdD terminates polymerization by adding a methyl phosphate to the non-reducing end of the nascent O9a polymer. The O9a system is a representative of the widespread ATP-binding cassette transporter-dependent assembly pathway. This terminal modification is required for recognition and export of the completed O-PS across the cytoplasmic membrane by its cognate ATP-binding cassette transporter. The recognition event is mediated by the nucleotide-binding domain polypeptide of the transporter, which possesses a serotype-specific carbohydrate-binding module that only binds terminated O-PS chains. The WbdD terminator plays an additional pivotal structural role in recruiting WbdA to the membrane. The stoichiometry of WbdA:WbdD in active complexes is a critical factor in establishing the chain length distribution of the resulting glycans. The size of the O9a polysaccharide is determined by the chain-terminating dual kinase/methyltransferase (WbdD) that is tethered to the membrane and recruits polymerase/glycosyltransferase WbdA into an active enzyme complex by protein-protein interactions. Identification via bacterial two-hybrid analysis of a surface-exposed alpha-helix in the C-terminal mannosyltransferase domain of WbdA as the site of interaction with WbdD, the C-terminal domain was unable to interact with WbdD in the absence of its N-terminal partner. The WbdD protein orchestrates critical localization and coordination of activities involved in chain extension and termination. Complex domain interactions are needed to position the polymerase components appropriately for assembly into a functional complex located at the cytoplasmic membrane. WbdD is therefore a central player in a sophisticated quality control system that dictates the distribution of chain lengths and marks those chains with a terminal export tag
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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722733
Clarke
In vitro reconstruction of the ...
Escherichia coli, Escherichia coli O9a
J. Biol. Chem.
286
41391-41401
2011
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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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722640
Clarke
Nonreducing terminal modificat ...
Escherichia coli, Escherichia coli O9a
J. Biol. Chem.
279
35709-35718
2004
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