STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
lpxBlipid-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. (389 aa)    
Predicted Functional Partners:
lpxA
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.
 
  
 0.995
lpxD
UDP-3-O-(3-hydroxymyristoyl) glucosamine N-acyltransferase; Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3- hydroxyacyl-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. Belongs to the transferase hexapeptide repeat family. LpxD subfamily.
 
 
 0.991
lpxK
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).
 
  
 0.985
rnhB
Ribonuclease H; Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
  
  
 0.959
lpxH
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.
 
  
 0.958
Bphy_0331
KpsF/GutQ family protein; KEGG: bxe:Bxe_A4117 KpsF/GutQ; TIGRFAM: KpsF/GutQ family protein; PFAM: CBS domain containing protein; sugar isomerase (SIS); Belongs to the SIS family. GutQ/KpsF subfamily.
 
   
 0.887
lpxC
UDP-3-0-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; Belongs to the LpxC family.
 
   
 0.863
Bphy_2264
Three-deoxy-D-manno-octulosonic-acid transferase domain protein; Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP- Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A; Belongs to the glycosyltransferase group 1 family.
 
   
 0.862
kdsB
3-deoxy-D-manno-octulosonate cytidylyltransferase; Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
 
   
 0.857
kdsA
TIGRFAM: 2-dehydro-3-deoxyphosphooctonate aldolase; PFAM: DAHP synthetase I/KDSA; KEGG: bxe:Bxe_A1572 2-dehydro-3-deoxyphosphooctonate aldolase.
 
   
 0.854
Your Current Organism:
Paraburkholderia phymatum
NCBI taxonomy Id: 391038
Other names: Burkholderia phymatum STM815, Burkholderia sp. STM815, P. phymatum STM815, Paraburkholderia phymatum STM815
Server load: low (34%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.