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.
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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Co-occurrence
Co-expression
Experiments
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[Homology]
Score
ysnEPutative indole acetic acid acetyltransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the acetyltransferase family. (151 aa)    
Predicted Functional Partners:
yhcX
Putative amidohydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the carbon-nitrogen hydrolase superfamily. NIT1/NIT2 family.
  
  
 0.934
dhaS
Putative aldehyde dehydrogenase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the aldehyde dehydrogenase family.
      
 0.903
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.
      
 0.783
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.
      
 0.716
alsR
Transcriptional regulator controlling alsSD and ictEP expression (LysR family); Regulates the expression of the alsSD operon for acetoin biosynthesis.
   
  
 0.677
alsD
Alpha-acetolactate decarboxylase; Converts acetolactate into acetoin, which can be excreted by the cells. This may be a mechanism for controlling the internal pH of cells in the stationary stage; Belongs to the alpha-acetolactate decarboxylase family.
      
 0.640
yotD
Hypothetical protein; Evidence 5: No homology to any previously reported sequences.
      
 0.639
alkA
DNA-3-methyladenine glycosylase; Is involved in the adaptive response to alkylation damage in DNA caused by alkylating agents. Catalyzes the hydrolysis of the deoxyribose N-glycosidic bond to excise 3-methyladenine and 7- methylguanine from the damaged DNA polymer formed by alkylation lesions.
  
    0.577
alsS
Alpha-acetolactate synthase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme.
      
 0.566
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.
   
  
 0.565
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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