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
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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[Homology]
Score
BF49_1255ABC transporter HlyBMsbA family. (651 aa)    
Predicted Functional Partners:
hemH
Ferrochelatase protoheme ferrolyase EC 49911; Catalyzes the ferrous insertion into protoporphyrin IX. Belongs to the ferrochelatase family.
   
 
 0.726
BF49_4284
ABCtype multidrug transport system ATPase and permease components.
  
 
0.698
BF49_1936
ABC transporter HlyBMsbA family.
  
 
0.695
BF49_6223
Phospholipidlipopolysaccharide ABC transporter.
  
 
0.695
BF49_5713
Lipid A export ATPbindingpermease protein MsbA.
  
 
0.690
psd
Phosphatidylserine decarboxylase EC 41165; Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
       0.645
ndvA
Beta12glucan export ATPbindingpermease protein NdvA EC 36342; Involved in Beta-(1-->2)glucan export. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
    
 0.644
BF49_5035
Transport ATPbinding protein CydCD.
    
 0.644
BF49_0718
Ironsulfur cluster assembly protein SufD.
   
 0.625
BF49_0720
Ironsulfur cluster assembly protein SufB.
   
 0.625
Your Current Organism:
Bradyrhizobium sp.
NCBI taxonomy Id: 376
Other names: B. sp.
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