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
Your Input:
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[Homology]
Score
ybxIExported beta-lactamase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (267 aa)    
Predicted Functional Partners:
dacB
D-alanyl-D-alanine carboxypeptidase (penicillin-binding protein 5*); Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors. Required specifically for the synthesis of the spore form of peptidoglycan (cortex).
      
 0.977
yodJ
D-alanyl-D-alanine carboxypeptidase lipoprotein; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme.
      
 0.923
cypC
Fatty acid beta-hydroxylating cytochrome P450; Catalyzes the alpha- and beta-hydroxylation of myristic acid in the presence of hydrogen peroxide; Belongs to the cytochrome P450 family.
       0.511
penP
Beta-lactamase precursor; This protein is a beta-lactamase with a substrate specificity for penicillins.
 
   
 0.404
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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