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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[Homology]
Score
thiNThiamine pyrophosphokinase; Catalyzes the phosphorylation of thiamine to thiamine pyrophosphate. (214 aa)    
Predicted Functional Partners:
tenA
Thiaminase II; Catalyzes an amino-pyrimidine hydrolysis reaction at the C5' of the pyrimidine moiety of thiamine compounds, a reaction that is part of a thiamine salvage pathway. Thus, catalyzes the conversion of 4- amino-5-aminomethyl-2-methylpyrimidine to 4-amino-5-hydroxymethyl-2- methylpyrimidine (HMP). To a lesser extent, is also able to catalyze the hydrolytic cleavage of thiamine; however, this thiaminase activity is unlikely to be physiologically relevant. Therefore, is involved in the regeneration of the thiamine pyrimidine from thiamine degraded products present in the enviro [...]
    
 0.992
cpgA
GTPase involved in ribosome and sacculus morphogenesis; One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase with a low level of activity and slow catalytic turnover, does not act on ATP. GTPase activity is stimulated by the presence of 30S or 70S ribosomes, phosphorylation increases stimulation. Depletion results in increased sensitivity to protein synthesis inhibitors that block the [...]
  
 
 0.988
thiL
tRNA-Asp; Catalyzes the ATP-dependent phosphorylation of thiamine- monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1; Belongs to the thiamine-monophosphate kinase family.
   
 
 0.974
pdxK
Pyridoxine, pyridoxal, and pyridoxamine kinase; Phosphorylates B6 vitamers; functions in a salvage pathway. Uses pyridoxal, pyridoxine, and pyridoxamine as substrates. Can also use hydroxymethylpyrimidine (HMP) as substrate. Belongs to the ThiD family.
     
 0.914
adk
Adenylate kinase; Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism; Belongs to the adenylate kinase family.
     
 0.910
thiE
Thiamine-phosphate pyrophosphorylase; Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP). Is also able to use the 2-methoxy analog MeO-HMP-PP, as substrate in vitro, but not the 2-trifluoromethyl analog CF(3)-HMP-PP. Belongs to the thiamine-phosphate synthase family.
     
 0.903
phoB
Alkaline phosphatase III; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the alkaline phosphatase family.
     
  0.900
phoA
Alkaline phosphatase A; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the alkaline phosphatase family.
     
  0.900
thiM
Hydroxyethylthiazole kinase; Catalyzes the phosphorylation of the hydroxyl group of 4- methyl-5-beta-hydroxyethylthiazole (THZ).
     
 0.881
prpC
Phosphorylated protein phosphatase; Protein phosphatase that dephosphorylates PrkC and EF-G (elongation factor G, fusA). prpC and prkC are cotranscribed, which suggests that they form a functional couple in vivo, PrpC's primary role being possibly to counter the action of PrkC. May be involved in sporulation and biofilm formation. Does not seem to be involved in stress response. Dephosphorylates phosphorylated CgsA, EF-Tu and YezB.
  
  
 0.876
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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