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
lpxAacyl-(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. (259 aa)    
Predicted Functional Partners:
lpxC
Beta-hydroxyacyl-(acyl-carrier-protein) dehydratase FabZ; 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 thioester dehydratase family. FabZ subfamily.
 
 0.999
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.
 
0.974
Amuc_2052
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.
 
  
 0.956
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).
 
   
 0.921
murA
UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Cell wall formation. Adds enolpyruvyl to UDP-N- acetylglucosamine; Belongs to the EPSP synthase family. MurA subfamily.
  
 
 0.861
Amuc_0474
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.
 
   
 0.816
rpsB
PFAM: ribosomal protein S2; KEGG: pha:PSHAa2036 30S ribosomal subunit protein S2; Belongs to the universal ribosomal protein uS2 family.
 
  
 0.800
Amuc_1541
PFAM: lipid A biosynthesis acyltransferase; KEGG: hha:Hhal_2316 lipid A biosynthesis lauroyl (or palmitoleoyl) acyltransferase.
 
   
 0.778
Amuc_0179
TIGRFAM: HAD-superfamily hydrolase, subfamily IA, variant 3; HAD-superfamily hydrolase, subfamily IA, variant 1; PFAM: Haloacid dehalogenase domain protein hydrolase; KEGG: dvu:DVU0130 phosphoglycolate phosphatase, putative.
       0.773
kdsB
3-deoxy-D-manno-octulosonate cytidylyltransferase; Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
 
   
 0.746
Your Current Organism:
Akkermansia muciniphila
NCBI taxonomy Id: 349741
Other names: A. muciniphila ATCC BAA-835, Akkermansia muciniphila ATCC BAA-835, Akkermansia muciniphila Muc, Akkermansia muciniphila str. ATCC BAA-835, Akkermansia muciniphila strain ATCC BAA-835, Akkermansia sp. Muc
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.