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Information on EC 2.7.8.43 - lipid A phosphoethanolamine transferase

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EC Tree
IUBMB Comments
The enzyme adds one or two ethanolamine phosphate groups to lipid A giving a diphosphate, sometimes in combination with EC 2.4.2.43 (lipid IVA 4-amino-4-deoxy-L-arabinosyltransferase) giving products with 4-amino-4-deoxy-beta-L-arabinose groups at the phosphates of lipid A instead of diphosphoethanolamine groups. It will also act on lipid IVA and Kdo2-lipid A.
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UNIPROT: P0ADV1
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Word Map
  • 2.7.8.43
  • colistin-resistant
  • plasmid-mediated
  • last-resort
  • kdo
  • last-line
  • 3-deoxy-d-manno-octulosonic
  • synthesis
The enzyme appears in viruses and cellular organisms
Synonyms
phosphoethanolamine transferase, petn transferase, pea transferase, lipid a phosphoethanolamine transferase, cj0256, esa_rs09200, lipooligosaccharide phosphoethanolamine transferase a, hp0022, lpt-o, phosphoethanolamine transferase a, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
lipid A PEA transferase
-
-
-
-
LptA
-
-
-
-
PmrA
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-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
diacylphosphatidylethanolamine:lipid-A phosphoethanolaminetransferase
The enzyme adds one or two ethanolamine phosphate groups to lipid A giving a diphosphate, sometimes in combination with EC 2.4.2.43 (lipid IVA 4-amino-4-deoxy-L-arabinosyltransferase) giving products with 4-amino-4-deoxy-beta-L-arabinose groups at the phosphates of lipid A instead of diphosphoethanolamine groups. It will also act on lipid IVA and Kdo2-lipid A.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
additional information
?
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
LptA is a member of the lipopolysaccharide transport protein (Lpt) family
malfunction
a mutant LptA protein unable to form oligomers has an altered affinity for LPS
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LPTA_ECOLI
Escherichia coli (strain K12)
185
0
20127
Swiss-Prot
Secretory Pathway (Reliability: 1)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oligomer
the enzyme LptA arranges in an end-to-end fibrous tetramer, which forms a continuous hydrophobic groove between the LptA monomers, crystal structure analysis. Mass spectral analysis confirmes that LptA forms 2-5-member oligomers in a concentration-dependent manner when purified in vitro and that the resultant complexes are stabilized by LPS. Analysis of subunit interactions
additional information
according to light scattering data, LptA oligomerizes in a concentration-dependent manner. LptA is an average of a trimer in solution, and a considerably higher order oligomerization state (25mers) is predicted at a protein concentration of 0.1 mM
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
I36R1
site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type
I36R1/Q148A/K149A
site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type
I86R1
site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type
I86R1/Q148A/K149A
site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type
L145R1
site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type
L45R1
site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type
M98R1
site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type
N185R1
site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type
N185R1/Q148A/K149A
site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type
Q148A/K149A
site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type
S110R1
site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type
T32R1
site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type
V132R1
site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type
V165R1
site-directed mutagenesis, altered lipopolysaccharide binding kinetics compared to wild-type
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant C-terminally His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3)pLysS by cobalt affinity chromatography, dialysis, and ultrafiltration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene lptA, recombinant expression of C-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)pLysS
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hicks, G.; Jia, Z.
Structural basis for the lipopolysaccharide export activity of the bacterial lipopolysaccharide transport system
Int. J. Mol. Sci.
19
E2680
2018
Escherichia coli (P0ADV1)
Manually annotated by BRENDA team
Schultz, K.M.; Lundquist, T.J.; Klug, C.S.
Lipopolysaccharide binding to the periplasmic protein LptA
Protein Sci.
26
1517-1523
2017
Escherichia coli (P0ADV1)
Manually annotated by BRENDA team