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.
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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
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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.
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from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
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gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
Lrub_2033Lysophospholipase A. (307 aa)    
Predicted Functional Partners:
Lrub_2034
ATPases involved in biogenesis of archaeal flagella.
       0.719
lapB
Tetratricopeptide repeat protein; Modulates cellular lipopolysaccharide (LPS) levels by regulating LpxC, which is involved in lipid A biosynthesis. May act by modulating the proteolytic activity of FtsH towards LpxC. May also coordinate assembly of proteins involved in LPS synthesis at the plasma membrane; Belongs to the LapB family.
      
 0.598
Lrub_2032
Hypothetical protein.
       0.518
lspD
Type II protein secretion LspD.
   
  
 0.472
lspF
Type II secretory pathway protein LspF.
      
 0.429
lspK
Type II secretory pathway protein LspK.
      
 0.429
lipB
Lipoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
      
 0.429
Lrub_0053
Type 4 (IV) prepilin-like protein leader peptide processing enzyme PilD; Cleaves type-4 fimbrial leader sequence and methylates the N- terminal (generally Phe) residue.
      
 0.429
lipA
Lipoyl synthase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
      
 0.429
Lrub_1611
Aminopeptidase.
  
     0.417
Your Current Organism:
Legionella rubrilucens
NCBI taxonomy Id: 458
Other names: ATCC 35304, CCUG 29671, CIP 103848, DSM 11884, JCM 7565, L. rubrilucens, NCTC 11987, strain WA-270A-C2
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