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
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Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
bsdAHTH-type transcriptional regulator BsdA (LysR family); Could be a positive regulator of bsdBCD expression in response to salicylic acid. (290 aa)    
Predicted Functional Partners:
padC
Phenolic acid decarboxylase; Involved in the decarboxylation and detoxification of phenolic derivatives. It is able to catalyze the decarboxylation of ferulic, p-coumaric and caffeic acids; Belongs to the PadC family.
      
 0.847
tcyB
Cystine ABC transporter (permease); Part of the ABC transporter complex TcyABC involved in L- cystine import. Probably responsible for the translocation of the substrate across the membrane (Probable). Belongs to the binding-protein-dependent transport system permease family.
  
  
 0.786
tcyC
Cystine ABC transporter (ATP-binding protein); Part of the ABC transporter complex TcyABC involved in L- cystine import. Responsible for energy coupling to the transport system (Probable).
  
  
 0.774
tcyA
Cystine ABC transporter (substrate-binding lipoprotein); Part of the ABC transporter complex TcyABC involved in L- cystine import.
  
  
 0.708
bsdB
Phenolic acid decarboxylase subunit BsdB; Involved in the non-oxidative decarboxylation and detoxification of phenolic derivatives under both aerobic and anaerobic conditions. Flavin prenyltransferase that catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for phenolic acid decarboxylase (By similarity); Belongs to the UbiX/PAD1 family. YclB subfamily.
  
  
 0.622
bsdC
Phenolic acid decarboxylase subunit BsdC; Involved in the non-oxidative decarboxylation and detoxification of phenolic derivatives under both aerobic and anaerobic conditions. Phenolic acid decarboxylase that catalyzes the reversible decarboxylation of 4- hydroxybenzoate and vanillate. Could also catalyze the decarboxylation of salicylate (Probable). Is not active on di- and tri-hydroxybenzoate derivatives. Belongs to the UbiD family. YclC subfamily.
  
  
 0.611
yczE
N-terminal part of 4'-phosphopantetheinyl transferase (Surfactin synthetase-activating enzyme); Evidence 7: Gene remnant; Product type e: enzyme.
     
 0.575
bsdD
Phenolic acid decarboxylase subunit BsdD; Involved in the non-oxidative decarboxylation and detoxification of phenolic derivatives under both aerobic and anaerobic conditions, however the precise biochemical function of BsdD in metabolism of phenolic acid is unknown.
       0.518
yclD
Putative FMN-binding enzyme subunit; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme.
       0.518
yvaB
NADH:dichloroindophenol oxidoreductase; Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADH, but not NADPH, as an electron donor for its activity. Confers resistance to catechol, 2- methylhydroquinone (2-MHQ), and diamide. Probably could also reduce benzoquinones produce by the auto-oxidation of catechol and 2- methylhydroquinone.
  
  
 0.485
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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