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Information on EC 2.7.1.235 - lipopolysaccharide core heptose(I) kinase
for references in articles please use BRENDA:EC2.7.1.235
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EC Tree 2 Transferases
2.7 Transferring phosphorus-containing groups
2.7.1 Phosphotransferases with an alcohol group as acceptor
2.7.1.235 lipopolysaccharide core heptose(I) kinase
IUBMB Comments
The enzyme catalyses the phosphorylation of L-glycero-D-manno-heptose I (the first heptose added to the lipid, Hep I) in the biosynthesis of the inner core oligosaccharide of the lipopolysaccharide (endotoxin) of some Gram-negative bacteria.
The enzyme appears in viruses and cellular organisms
Reaction Schemes
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Synonyms
RfaP, WaaP, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
RfaP
WaaP
RfaP
-
-
-
-
WaaP
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + an alpha-Hep-(1->3)-alpha-Hep-(1->5)-[alpha-Kdo-(2->4)]-alpha-Kdo-(2->6)-[lipid A] = ADP + an alpha-Hep-(1->3)-4-O-phospho-alpha-Hep-(1->5)-[alpha-Kdo-(2->4)]-alpha-Kdo-(2->6)-[lipid A]
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
lipid A-core biosynthesis (E. coli K-12), lipid A-core biosynthesis (Salmonella)
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SYSTEMATIC NAME
IUBMB Comments
ATP:an alpha-Hep-(1->3)-alpha-Hep-(1->5)-[alpha-Kdo-(2->4)]-alpha-Kdo-(2->6)-[lipid A] heptoseI 4-O-phosphotransferase
The enzyme catalyses the phosphorylation of L-glycero-D-manno-heptose I (the first heptose added to the lipid, Hep I) in the biosynthesis of the inner core oligosaccharide of the lipopolysaccharide (endotoxin) of some Gram-negative bacteria.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + an alpha-Hep-(1->3)-alpha-Hep-(1->5)-[alpha-Kdo-(2->4)]-alpha-Kdo-(2->6)-[lipid A]
ADP + an alpha-Hep-(1->3)-4-O-phospho-alpha-Hep-(1->5)-[alpha-Kdo-(2->4)]-alpha-Kdo-(2->6)-[lipid A]
Substrates: -
Products: -
Products: -
?
ATP + [hydrofluoric acid-treated lipopolysaccharide]
ADP + phospho-[hydrofluoric acid-treated lipopolysaccharide]
ATP + [hydrofluoric acid-treated lipopolysaccharide]
ADP + phospho-[hydrofluoric acid-treated lipopolysaccharide]
Substrates: -
Products: -
Products: -
?
ATP + [hydrofluoric acid-treated lipopolysaccharide]
ADP + phospho-[hydrofluoric acid-treated lipopolysaccharide]
Substrates: -
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + an alpha-Hep-(1->3)-alpha-Hep-(1->5)-[alpha-Kdo-(2->4)]-alpha-Kdo-(2->6)-[lipid A]
ADP + an alpha-Hep-(1->3)-4-O-phospho-alpha-Hep-(1->5)-[alpha-Kdo-(2->4)]-alpha-Kdo-(2->6)-[lipid A]
Substrates: -
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
activity is absolutely dependent upon the presence of Mg2+, maximum activity at 17.5 mM
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
myristoyl-ACP
myristoyl-ACP is the likely physiological binding partner for WaaP
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.076
an alpha-Hep-(1->3)-alpha-Hep-(1->5)-[alpha-Kdo-(2->4)]-alpha-Kdo-(2->6)-[lipid A]
pH 7.5, 35°C
0.014
[hydrofluoric acid-treated lipopolysaccharide]
pH 7.5, 37°C
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
WaaP is required for the addition of phosphate to O-4 of the first heptose residue of the lipopolysaccharide inner core region. WaaP is necessary for resistance to hydrophobic and polycationic antimicrobials in Escherichia coli
physiological function
WaaP protein is a sugar kinase that adds phosphate to heptose I in the core oligosaccharide of lipopolysaccharide
physiological function
-
WaaP protein is a sugar kinase that adds phosphate to heptose I in the core oligosaccharide of lipopolysaccharide
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). WAAP_ECOLI
Escherichia coli (strain K12)
265
0
30872
Swiss-Prot
other Location (Reliability: 1)
WAAP_SALTY
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
265
0
30996
Swiss-Prot
-
WAAP_PSEAE
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
268
0
31311
Swiss-Prot
other Location (Reliability: 2)
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 31049, calculated from sequence, x * 33000, SDS-PAGE of recombinant His-tagged protein
?
x * 32900, calculated from sequence, x * 33000, SDS-PAGE, both of recombinant His-tagged protein
?
-
x * 32900, calculated from sequence, x * 33000, SDS-PAGE, both of recombinant His-tagged protein
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphoprotein
all eight tyrosine residues in WaaP may be phosphorylated
phosphoprotein
-
all eight tyrosine residues in WaaP may be phosphorylated
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure in complex with acylated-acyl carrier protein (acyl-ACP)
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A214F
mutation in mid pocket, able to grow in an EDTA resistance assay
A214L
mutation in mid pocket, able to grow in an EDTA resistance assay
A214W
mutation in mid pocket, able to grow in an EDTA resistance assay
D163A
D163E
mutant is not able to complement an Escherichia coli WaaP mutant strain
D188N
mutation in ATP binding, no growth in an EDTA resistance assay
E78A
mutation in ATP binding, able to grow in an EDTA resistance assay
H161A
mutation in HRD motif, no growth in an EDTA resistance assay
H168A
mutation in substrate binding, no growth in an EDTA resistance assay
K51A
mutation in ATP binding, no growth in an EDTA resistance assay
K69A
K69R
mutant is not able to complement an Escherichia coli WaaP mutant strain
L143W
mutation in lipid terminus, able to grow in an EDTA resistance assay
L219W
mutation in mid pocket, able to grow in an EDTA resistance assay
L228A
mutation in pocket proximal to phosphopentatheine, able to grow in an EDTA resistance assay
L228W
mutation in pocket proximal to phosphopentatheine, able to grow in an EDTA resistance assay
R162A
mutation in HRD motif, able to grow in an EDTA resistance assay
R191A
mutation in substrate binding, no growth in an EDTA resistance assay
R221E/R222E/R226E/R229E/R237E
mutation in ACP binding, no growth in an EDTA resistance assay
R222A
mutation in ACP binding, able to grow in an EDTA resistance assay
R222A/R226A
mutation in ACP binding, able to grow in an EDTA resistance assay
R222E
mutation in ACP binding, able to grow in an EDTA resistance assay
R222E/R226E
mutation in ACP binding, able to grow in an EDTA resistance assay
R222E/R226E/R237E
mutation in ACP binding, able to grow in an EDTA resistance assay
R226A
mutation in ACP binding, able to grow in an EDTA resistance assay
R226E
mutation in ACP binding, able to grow in an EDTA resistance assay
S127L
mutation in lipid terminus, able to grow in an EDTA resistance assay
T198A
mutation in phosphorylation site, able to grow in an EDTA resistance assay
V147L
mutation in mid pocket, able to grow in an EDTA resistance assay
V147L/L219W
mutation in mid pocket, able to grow in an EDTA resistance assay
V147W
mutation in mid pocket, no growth in an EDTA resistance assay
V147W/214F
mutation in mid pocket, no growth in an EDTA resistance assay
Y165A
mutation in substrate binding, no growth in an EDTA resistance assay
D163A
-
mutant is not able to complement an Escherichia coli WaaP mutant strain
-
D163E
-
mutant is not able to complement an Escherichia coli WaaP mutant strain
-
D188N
-
mutation in ATP binding, no growth in an EDTA resistance assay
-
E78A
-
mutation in ATP binding, able to grow in an EDTA resistance assay
-
K51A
-
mutation in ATP binding, no growth in an EDTA resistance assay
-
K69A
K69R
-
mutant is not able to complement an Escherichia coli WaaP mutant strain
-
additional information
D163A
mutant is not able to complement an Escherichia coli WaaP mutant strain
D163A
mutation in HRD motif, no growth in an EDTA resistance assay
K69A
mutant is not able to complement an Escherichia coli WaaP mutant strain
K69A
mutation in substrate binding, able to grow in an EDTA resistance assay
K69A
-
mutant is not able to complement an Escherichia coli WaaP mutant strain
-
K69A
-
mutation in substrate binding, able to grow in an EDTA resistance assay
-
additional information
WaaP produced by in vitro transcription-translation is insoluble unless acyl-ACP is present. WaaP variants designed to perturb the acyl-ACP interaction are less stable in cells and exhibit reduced kinase function
additional information
-
WaaP produced by in vitro transcription-translation is insoluble unless acyl-ACP is present. WaaP variants designed to perturb the acyl-ACP interaction are less stable in cells and exhibit reduced kinase function
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant protein, purified by immobilized metal affinity chromatography and subtractive anion exchange chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli. WaaP produced by in vitro transcription-translation is insoluble unless acyl-ACP is present
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
analysis
chemiluminescence-based enzyme-linked immunosorbent assay for the detection of WaaP kinase activity. The assay displays high sensitivity, uses dephosphorylated LPS as a substrate, and monoclonal antibody 7-4 that specifically recognizes phosphate substituents in the LPS core
analysis
-
chemiluminescence-based enzyme-linked immunosorbent assay for the detection of WaaP kinase activity. The assay displays high sensitivity, uses dephosphorylated LPS as a substrate, and monoclonal antibody 7-4 that specifically recognizes phosphate substituents in the LPS core
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yethon, J.A.; Whitfield, C.
Purification and characterization of WaaP from Escherichia coli, a lipopolysaccharide kinase essential for outer membrane stability
J. Biol. Chem.
276
5498-5504
2001
Escherichia coli (Q9R9D6)
brenda
Zhao, X.; Wenzel, C.; Lam, J.
Nonradiolabeling assay for WaaP, an essential sugar kinase involved in biosynthesis of core lipopolysaccharide of Pseudomonas aeruginosa
Antimicrob. Agents Chemother.
46
2035-2037
2002
Pseudomonas aeruginosa (Q9HUF7), Pseudomonas aeruginosa DSM 22644 (Q9HUF7)
brenda
Zhao, X.; Lam, J.
WaaP of Pseudomonas aeruginosa is a novel eukaryotic type protein-tyrosine kinase as well as a sugar kinase essential for the biosynthesis of core lipopolysaccharide
J. Biol. Chem.
277
4722-4730
2002
Pseudomonas aeruginosa (Q9HUF7), Pseudomonas aeruginosa DSM 22644 (Q9HUF7)
brenda
Kreamer, N.; Chopra, R.; Caughlan, R.; Fabbro, D.; Fang, E.; Gee, P.; Hunt, I.; Li, M.; Leon, B.; Muller, L.; Vash, B.; Woods, A.; Stams, T.; Dean, C.; Uehara, T.
Acylated-acyl carrier protein stabilizes the Pseudomonas aeruginosa WaaP lipopolysaccharide heptose kinase
Sci. Rep.
8
14124
2018
Pseudomonas aeruginosa (Q9HUF7), Pseudomonas aeruginosa DSM 22644 (Q9HUF7)
brenda
EXTERNAL LINKS (specific for EC-Number 2.7.1.235)
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