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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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Co-expression
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[Homology]
Score
lpxAacyl-[acyl-carrier-protein]--UDP-N-acetylglucosa mine O-acyl; Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. (255 aa)    
Predicted Functional Partners:
fabZ
(3R)-hydroxymyristoyl-[acyl carrier protein] dehydratase; Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
  
 0.997
lpxB
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.
 
  
 0.996
lpxD
UDP-3-O-[3-hydroxymyristoyl] glucosamineN-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
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.
 
 
 0.987
rnhB
Ribonuclease H; Endonuclease that specifically degrades the RNA of RNA-DNA hybrids; Belongs to the RNase HII family.
  
  
 0.926
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).
 
   
 0.919
waaA
3-deoxy-D-manno-octulosonic-acid transferase; 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.
 
   
 0.911
murA
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Cell wall formation. Adds enolpyruvyl to UDP-N- acetylglucosamine; Belongs to the EPSP synthase family. MurA subfamily.
  
 
 0.907
dnaE
DNA polymerase III, alpha subunit; Identified by match to PFAM protein family HMMPF02811 InterPro: DNA polymerase III alpha subunit; High confidence in function and specificity.
    
 0.891
kdsA-1
2-dehydro-3-deoxyphosphooctonate aldolase; Identified by match to PFAM protein family HMMPF00793 2-dehydro-3-deoxyphosphooctonate aldolase (EC 2.5.1.55) (phospho-2- dehydro-3-deoxyoctonate aldolase) (3-deoxy-d-manno-octulosonic acid 8- phosphate synthetase) (kdo-8-phosphate synthetase) (kdo 8-p synthase) (kdops); High confidence in function and specificity; Belongs to the KdsA family.
 
   
 0.868
Your Current Organism:
Alcanivorax borkumensis
NCBI taxonomy Id: 393595
Other names: A. borkumensis SK2, Alcanivorax borkumensis SK2, Alcanivorax borkumensis str. SK2, Alcanivorax borkumensis strain SK2
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.