BRENDA - Enzyme Database show
show all sequences of 2.7.8.43

Crystallographic study of the phosphoethanolamine transferase EptC required for polymyxin resistance and motility in Campylobacter jejuni

Fage, C.D.; Brown, D.B.; Boll, J.M.; Keatinge-Clay, A.T.; Trent, M.S.; Acta Crystallogr. Sect. D 70, 2730-2739 (2014)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene eptC, recombinant expression of C-terminally Gly6-His8-tagged enzyme in Escherichia coli strain BL21(DE3), recombinant expression of His-tagged enzyme as selenomethionine-labeled enzyme
Campylobacter jejuni
Crystallization (Commentary)
Crystallization
Organism
purified recombinant His-tagged wild-type and selenomethionine-labeled enzyme EptC, sitting drop vapour diffusion method, mixing of 0.004 ml of 30 mg/ml protein in 25 mM NaCl, 10 mM HEPES, pH 7.5, with 0.001 ml of precipitant solution containing 200 mM diammonium phosphate, 15% w/v PEG 3350, 22C, X-ray diffraction structure determination and analysis at 2.40-2.80 A resolution, molecular replacement
Campylobacter jejuni
Engineering
Amino acid exchange
Commentary
Organism
H358A
site-directed mutagenesis, mutation of a potential zinc binding residue
Campylobacter jejuni
H440A
site-directed mutagenesis, mutation of a potential zinc binding residue
Campylobacter jejuni
N308A
site-directed mutagenesis, mutation of a potential zinc binding residue
Campylobacter jejuni
S309A
site-directed mutagenesis, mutation of a potential zinc binding residue
Campylobacter jejuni
T266A
site-directed mutagenesis, mutation of a potential zinc binding residue
Campylobacter jejuni
T266S
site-directed mutagenesis, mutation of a potential zinc binding residue
Campylobacter jejuni
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
inner membrane
phosphoethanolamine modification occurs on the periplasmic side of the inner membrane, where enzyme EptC transfers head groups from the phospholipid phosphoethanolamine to target molecules. EptC is predicted to be anchored to the inner membrane by a five-helix transmembrane domain, with its sulfatase-like catalytic domain positioned in the periplasm
Campylobacter jejuni
-
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Zn2+
zinc-binding residues of the phosphoenzyme intermediate, overview. The cEptC active site contains a tetrahedrally coordinated zinc ion and a putative nucleophilic threonine, Thr266, covalently bound to a phosphoryl group to form phosphothreonine
Campylobacter jejuni
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
36700
-
-
Campylobacter jejuni
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
diacylphosphatidylethanolamine + flagellar rod protein FlgG
Campylobacter jejuni
-
?
-
-
?
diacylphosphatidylethanolamine + flagellar rod protein FlgG
Campylobacter jejuni 81-176
-
?
-
-
?
diacylphosphatidylethanolamine + lipid A
Campylobacter jejuni
-
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
-
-
?
diacylphosphatidylethanolamine + lipid A
Campylobacter jejuni
-
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
-
?
diacylphosphatidylethanolamine + lipid A
Campylobacter jejuni 81-176
-
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
-
-
?
additional information
Campylobacter jejuni
pEtN transferase, EptC, modifies an array of cell-surface molecules and the N-linked glycans of numerous glycoproteins
?
-
-
-
additional information
Campylobacter jejuni 81-176
pEtN transferase, EptC, modifies an array of cell-surface molecules and the N-linked glycans of numerous glycoproteins
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Campylobacter jejuni
A0A1B3XBZ7
-
-
Campylobacter jejuni 81-176
A0A1B3XBZ7
-
-
Posttranslational Modification
Posttranslational Modification
Commentary
Organism
phosphoprotein
the cEptC active site contains a putative nucleophilic threonine, Thr266, covalently bound to a phosphoryl group to form phosphothreonine. Phospho-Thr266 mimics an enzyme reaction intermediate representing the first step in a two-step transferase reaction
Campylobacter jejuni
Purification (Commentary)
Commentary
Organism
recombinant His-tagged wild-type and selenomethionine-labeled enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
Campylobacter jejuni
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
diacylphosphatidylethanolamine + flagellar rod protein FlgG
-
739786
Campylobacter jejuni
?
-
-
-
?
diacylphosphatidylethanolamine + flagellar rod protein FlgG
EptC transfers phosphoethanolamine from the head groups of phosphatidylethanolamine onto Thr75 of FlgG proteins
739786
Campylobacter jejuni
?
-
-
-
?
diacylphosphatidylethanolamine + flagellar rod protein FlgG
-
739786
Campylobacter jejuni 81-176
?
-
-
-
?
diacylphosphatidylethanolamine + flagellar rod protein FlgG
EptC transfers phosphoethanolamine from the head groups of phosphatidylethanolamine onto Thr75 of FlgG proteins
739786
Campylobacter jejuni 81-176
?
-
-
-
?
diacylphosphatidylethanolamine + lipid A
-
739786
Campylobacter jejuni
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + lipid A
EptC transfers phosphoethanolamine from the head groups of phosphatidylethanolamine onto the LOS core and phosphates of lipid A
739786
Campylobacter jejuni
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + lipid A
-
739786
Campylobacter jejuni 81-176
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + lipid A
EptC transfers phosphoethanolamine from the head groups of phosphatidylethanolamine onto the LOS core and phosphates of lipid A
739786
Campylobacter jejuni 81-176
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + lipid A
-
739786
Campylobacter jejuni
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + lipid A
EptC transfers phosphoethanolamine from the head groups of phosphatidylethanolamine onto the LOS core and phosphates of lipid A
739786
Campylobacter jejuni
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
-
-
?
additional information
pEtN transferase, EptC, modifies an array of cell-surface molecules and the N-linked glycans of numerous glycoproteins
739786
Campylobacter jejuni
?
-
-
-
-
additional information
pEtN transferase, EptC, modifies an array of cell-surface molecules and the N-linked glycans of numerous glycoproteins
739786
Campylobacter jejuni 81-176
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
?
x * 36700, recombinant His-tagged wild-type, SDS-PAGE
Campylobacter jejuni
More
enzyme structure analysis, overview
Campylobacter jejuni
Cloned(Commentary) (protein specific)
Commentary
Organism
gene eptC, recombinant expression of C-terminally Gly6-His8-tagged enzyme in Escherichia coli strain BL21(DE3), recombinant expression of His-tagged enzyme as selenomethionine-labeled enzyme
Campylobacter jejuni
Crystallization (Commentary) (protein specific)
Crystallization
Organism
purified recombinant His-tagged wild-type and selenomethionine-labeled enzyme EptC, sitting drop vapour diffusion method, mixing of 0.004 ml of 30 mg/ml protein in 25 mM NaCl, 10 mM HEPES, pH 7.5, with 0.001 ml of precipitant solution containing 200 mM diammonium phosphate, 15% w/v PEG 3350, 22C, X-ray diffraction structure determination and analysis at 2.40-2.80 A resolution, molecular replacement
Campylobacter jejuni
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
H358A
site-directed mutagenesis, mutation of a potential zinc binding residue
Campylobacter jejuni
H440A
site-directed mutagenesis, mutation of a potential zinc binding residue
Campylobacter jejuni
N308A
site-directed mutagenesis, mutation of a potential zinc binding residue
Campylobacter jejuni
S309A
site-directed mutagenesis, mutation of a potential zinc binding residue
Campylobacter jejuni
T266A
site-directed mutagenesis, mutation of a potential zinc binding residue
Campylobacter jejuni
T266S
site-directed mutagenesis, mutation of a potential zinc binding residue
Campylobacter jejuni
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
inner membrane
phosphoethanolamine modification occurs on the periplasmic side of the inner membrane, where enzyme EptC transfers head groups from the phospholipid phosphoethanolamine to target molecules. EptC is predicted to be anchored to the inner membrane by a five-helix transmembrane domain, with its sulfatase-like catalytic domain positioned in the periplasm
Campylobacter jejuni
-
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Zn2+
zinc-binding residues of the phosphoenzyme intermediate, overview. The cEptC active site contains a tetrahedrally coordinated zinc ion and a putative nucleophilic threonine, Thr266, covalently bound to a phosphoryl group to form phosphothreonine
Campylobacter jejuni
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
36700
-
-
Campylobacter jejuni
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
diacylphosphatidylethanolamine + flagellar rod protein FlgG
Campylobacter jejuni
-
?
-
-
?
diacylphosphatidylethanolamine + flagellar rod protein FlgG
Campylobacter jejuni 81-176
-
?
-
-
?
diacylphosphatidylethanolamine + lipid A
Campylobacter jejuni
-
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
-
-
?
diacylphosphatidylethanolamine + lipid A
Campylobacter jejuni
-
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
-
?
diacylphosphatidylethanolamine + lipid A
Campylobacter jejuni 81-176
-
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
-
-
?
additional information
Campylobacter jejuni
pEtN transferase, EptC, modifies an array of cell-surface molecules and the N-linked glycans of numerous glycoproteins
?
-
-
-
additional information
Campylobacter jejuni 81-176
pEtN transferase, EptC, modifies an array of cell-surface molecules and the N-linked glycans of numerous glycoproteins
?
-
-
-
Posttranslational Modification (protein specific)
Posttranslational Modification
Commentary
Organism
phosphoprotein
the cEptC active site contains a putative nucleophilic threonine, Thr266, covalently bound to a phosphoryl group to form phosphothreonine. Phospho-Thr266 mimics an enzyme reaction intermediate representing the first step in a two-step transferase reaction
Campylobacter jejuni
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged wild-type and selenomethionine-labeled enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
Campylobacter jejuni
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
diacylphosphatidylethanolamine + flagellar rod protein FlgG
-
739786
Campylobacter jejuni
?
-
-
-
?
diacylphosphatidylethanolamine + flagellar rod protein FlgG
EptC transfers phosphoethanolamine from the head groups of phosphatidylethanolamine onto Thr75 of FlgG proteins
739786
Campylobacter jejuni
?
-
-
-
?
diacylphosphatidylethanolamine + flagellar rod protein FlgG
-
739786
Campylobacter jejuni 81-176
?
-
-
-
?
diacylphosphatidylethanolamine + flagellar rod protein FlgG
EptC transfers phosphoethanolamine from the head groups of phosphatidylethanolamine onto Thr75 of FlgG proteins
739786
Campylobacter jejuni 81-176
?
-
-
-
?
diacylphosphatidylethanolamine + lipid A
-
739786
Campylobacter jejuni
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + lipid A
EptC transfers phosphoethanolamine from the head groups of phosphatidylethanolamine onto the LOS core and phosphates of lipid A
739786
Campylobacter jejuni
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + lipid A
-
739786
Campylobacter jejuni 81-176
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + lipid A
EptC transfers phosphoethanolamine from the head groups of phosphatidylethanolamine onto the LOS core and phosphates of lipid A
739786
Campylobacter jejuni 81-176
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + lipid A
-
739786
Campylobacter jejuni
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + lipid A
EptC transfers phosphoethanolamine from the head groups of phosphatidylethanolamine onto the LOS core and phosphates of lipid A
739786
Campylobacter jejuni
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
-
-
?
additional information
pEtN transferase, EptC, modifies an array of cell-surface molecules and the N-linked glycans of numerous glycoproteins
739786
Campylobacter jejuni
?
-
-
-
-
additional information
pEtN transferase, EptC, modifies an array of cell-surface molecules and the N-linked glycans of numerous glycoproteins
739786
Campylobacter jejuni 81-176
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 36700, recombinant His-tagged wild-type, SDS-PAGE
Campylobacter jejuni
More
enzyme structure analysis, overview
Campylobacter jejuni
General Information
General Information
Commentary
Organism
evolution
the eptC gene (locus tag Cj0256) is clustered in a family of inner-membrane metalloenzymes (COG2194) containing a fivehelix transmembrane domain and a periplasmic catalytic domain that is currently grouped in the sulfatase family
Campylobacter jejuni
additional information
identification of identify zinc-ligand residues, a putative nucleophile and conserved active-site residues required for in vivo activity from the crystal structure, active-site architecture of cEptC, overview
Campylobacter jejuni
physiological function
the foodborne enteric pathogen Campylobacter jejuni decorates a variety of its cell-surface structures with phosphoethanolamine. Modifying lipid A with phosphoethanolamine promotes cationic antimicrobial peptide resistance. Modifications of the Campylobacter jejuni surface structures with phosphoethanolamine promote flagellar assembly, motility, cationic antimicrobial peptide resistance and host intestinal colonization
Campylobacter jejuni
General Information (protein specific)
General Information
Commentary
Organism
evolution
the eptC gene (locus tag Cj0256) is clustered in a family of inner-membrane metalloenzymes (COG2194) containing a fivehelix transmembrane domain and a periplasmic catalytic domain that is currently grouped in the sulfatase family
Campylobacter jejuni
additional information
identification of identify zinc-ligand residues, a putative nucleophile and conserved active-site residues required for in vivo activity from the crystal structure, active-site architecture of cEptC, overview
Campylobacter jejuni
physiological function
the foodborne enteric pathogen Campylobacter jejuni decorates a variety of its cell-surface structures with phosphoethanolamine. Modifying lipid A with phosphoethanolamine promotes cationic antimicrobial peptide resistance. Modifications of the Campylobacter jejuni surface structures with phosphoethanolamine promote flagellar assembly, motility, cationic antimicrobial peptide resistance and host intestinal colonization
Campylobacter jejuni
Other publictions for EC 2.7.8.43
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)
750867
Hicks
-
Structural basis for the lipo ...
Escherichia coli
Int. J. Mol. Sci.
19
E2680
2018
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752134
Schultz
Lipopolysaccharide binding to ...
Escherichia coli
Protein Sci.
26
1517-1523
2017
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738476
Liu
A phosphoethanolamine transfer ...
Cronobacter sakazakii, Cronobacter sakazakii BAA894
J. Appl. Microbiol.
121
1444-1456
2016
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733635
Handing
The lipooligosaccharide-modify ...
Neisseria gonorrhoeae, Neisseria gonorrhoeae FA 1090
Cell. Microbiol.
17
910-921
2015
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1
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1
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2
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4
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2
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735018
Trombley
Phosphoethanolamine transferas ...
Haemophilus ducreyi, Haemophilus ducreyi ATCC 700724
PLoS ONE
10
e0124373
2015
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1
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1
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7
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5
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5
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2
3
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739106
Nowicki
Extracellular zinc induces pho ...
Pseudomonas aeruginosa
Mol. Microbiol.
97
166-178
2015
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1
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1
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4
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1
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2
1
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740532
Telke
Functional genomics to discove ...
Shewanella algae, Shewanella algae MARS 14
Int. J. Antimicrob. Agents
46
648-652
2015
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1
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2
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1
1
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738368
Packiam
Phosphoethanolamine decoration ...
Neisseria gonorrhoeae, Neisseria gonorrhoeae FA 1090
Infect. Immun.
82
2170-2179
2014
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1
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2
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11
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2
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739495
Piek
The role of oxidoreductases in ...
Neisseria meningitidis, Neisseria meningitidis NMB
PLoS ONE
9
e106513
2014
1
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Resistance to the antimicrobia ...
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Phosphorylation of the lipid A ...
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