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
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
maaMaltose O-acetyltransferase; Catalyzes the CoA-dependent transfer of an acetyl group to maltose and other sugars. Acetylates glucose exclusively at the C6 position and maltose at the C6 position of the non-reducing end glucosyl moiety. Is able to acetylate maltooligosaccharides. (184 aa)    
Predicted Functional Partners:
yyaH
Putative lyase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme.
  
    0.777
ccpB
Transcriptional repressor of carbon supply (LacI family); Transcriptional regulator involved in catabolite repression of several operons.
  
    0.770
pcrB
Heptaprenylglyceryl-phosphate synthase; Prenyltransferase that catalyzes in vivo the transfer of the heptaprenyl moiety of heptaprenyl pyrophosphate (HepPP; 35 carbon atoms) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P), producing heptaprenylglyceryl phosphate (HepGP). This reaction is an ether-bond- formation step in the biosynthesis of archaea-type G1P-based membrane lipids found in Bacillales. To a much lesser extent, is also able to use geranyl diphosphate (GPP; C10) and geranylgeranyl diphosphate (GGPP; C20) as the prenyl donors, but not farnesyl pyrophosphate (FPP; C15). Ca [...]
     
 0.760
araM
Glycerol-1-phosphate dehydrogenase [NAD(P)+]; Catalyzes the NAD(P)H-dependent reduction of dihydroxyacetonephosphate (DHAP or glycerone phosphate) to glycerol 1- phosphate (G1P). The G1P thus generated is probably used for the synthesis of phosphoglycerolipids in Gram-positive bacterial species. Prefers NADH over NADPH as coenzyme. Is also able to catalyze the reverse reaction, i.e. the NAD(+)-dependent oxidation of G1P but not of G3P. Does not possess glycerol dehydrogenase activity.
      
 0.699
niaR
Transcriptional repressor of de novo NAD biosynthesis; In the presence of nicotinic acid represses transcription of the nadBCA and nifS-nadR operons. Also binds to DNA upstream of the niaP gene, probably regulating it as well. May bind nicotinic acid.
      0.638
phoB
Alkaline phosphatase III; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the alkaline phosphatase family.
  
  
 0.599
yvoF
Putative O-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 transferase hexapeptide repeat family.
  
   
0.523
exoA
Apurinic/apyrimidinic endonuclease; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme.
  
    0.457
pksJ
Polyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism.
  
  
 0.456
pksN
Polyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism.
  
  
 0.454
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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