lpxD protein (Escherichia coli K12 MG1655) - STRING interaction network
"lpxD" - UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase in Escherichia coli K12 MG1655
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
protein homology
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Gene Fusion
lpxDUDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase; Catalyzes the N-acylation of UDP-3-O- (hydroxytetradecanoyl)glucosamine using 3-hydroxytetradecanoyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. Prefers (3R)-3- hydroxytetradecanoyl-ACP over (3R)-3-hydroxyhexadecanoyl-ACP as the acyl donor in vitro, which is consistent with the structure of E.coli lipid A that contains over 95% (R)-3-hydroxytetradecanoate at the 2 and 2’ positions; Belongs to the transferase [...] (341 aa)    
Predicted Functional Partners:
Lipid-A-disaccharide synthase; Condensation of UDP-2,3-diacylglucosamine and 2,3- diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell; Belongs to the LpxB family (382 aa)
UDP-3-O-acyl-N-acetylglucosamine deacetylase; Catalyzes the hydrolysis of UDP-3-O-myristoyl-N- acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis (305 aa)
3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ; Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs (151 aa)
Chaperone protein Skp; Molecular chaperone that interacts specifically with outer membrane proteins, thus maintaining the solubility of early folding intermediates during passage through the periplasm. Required for the efficient release of OmpA from the inner membrane, the maintenance of its solubility in the periplasm, and, in association with lipopolysaccharide (LPS), for the efficient folding and insertion of OmpA into the outer membrane; Belongs to the Skp family (161 aa)
UDP-2,3-diacylglucosamine hydrolase; Hydrolyzes the pyrophosphate bond of UDP-2,3- diacylglucosamine to yield 2,3-diacylglucosamine 1-phosphate (lipid X) and UMP by catalyzing the attack of water at the alpha-P atom. Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. Is essential for E.coli growth. Does not cleave the unacylated UDP-GlcNAc, the mono-acylated UDP-3-O-(R)-3- hydroxymyristoyl-GlcNAc, and CDP-diacylglycerol; Belongs to the LpxH family (240 aa)
Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell (262 aa)
Tetraacyldisaccharide 4’-kinase; Transfers the gamma-phosphate of ATP to the 4’-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1- P) to form tetraacyldisaccharide 1,4’-bis-phosphate (lipid IVA) (328 aa)
Acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis; Belongs to the acyl carrier protein (ACP) family (78 aa)
3-deoxy-D-manno-octulosonic acid transferase; Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of two 3-deoxy-D-manno-octulosonate (Kdo) residues from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide- 1,4’-bisphosphate precursor of lipid A; Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 30 subfamily (425 aa)
Outer membrane protein assembly factor BamA; Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits. A lateral gate may open between the first and last strands of the BamA beta- barrel that allows substrate to insert into the outer membrane; comparison of the structures of complete and nearly complete Bam complexes show there is cons [...] (810 aa)
Your Current Organism:
Escherichia coli K12 MG1655
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli K12 MG1655, Escherichia coli K12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
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