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
ypjQPutative phosphatidylglycerophosphatase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; To B.subtilis YutG. (177 aa)    
Predicted Functional Partners:
ypjP
Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function.
  
    0.765
pssA
Phosphatidylserine synthase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the CDP-alcohol phosphatidyltransferase class-I family.
  
  
 0.743
ltaSC
Enzyme responsible for polyglycerolphosphate LTA synthesis; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the LTA synthase family.
   
  
 0.682
pgsA
CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase; This protein catalyzes the committed step to the synthesis of the acidic phospholipids; Belongs to the CDP-alcohol phosphatidyltransferase class-I family.
 
  
 0.661
ypkP
Putative acyltransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme.
  
  
 0.631
psd
Phosphatidylserine decarboxylase; Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer); Belongs to the phosphatidylserine decarboxylase family. PSD-B subfamily. Prokaryotic type I sub-subfamily.
     
 0.592
dfrA
Dihydrofolate reductase; Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity).
  
    0.573
thyB
Thymidylate synthase B; Catalyzes the reductive methylation of 2'-deoxyuridine-5'- monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by- product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.
  
    0.569
ugtP
UDP-glucose diacylglyceroltransferase; Processive glucosyltransferase involved in the biosynthesis of both the bilayer- and non-bilayer-forming membrane glucolipids. Is able to successively transfer up to three glucosyl residues to diacylglycerol (DAG), thereby catalyzing the formation of beta- monoglucosyl-DAG (3-O-(beta-D-glucopyranosyl)-1,2-diacyl-sn-glycerol), beta-diglucosyl-DAG (3-O-(beta-D-glucopyranosyl-beta-(1->6)-D- glucopyranosyl)-1,2-diacyl-sn-glycerol) and beta-triglucosyl-DAG (3-O- (beta-D-glucopyranosyl-beta-(1->6)-D-glucopyranosyl-beta-(1->6)-D- glucopyranosyl)-1,2-diac [...]
  
  
 0.475
ppaX
P-Ser-HPr phosphatase; Hydrolyzes pyrophosphate formed during P-Ser-HPr dephosphorylation by HPrK/P. Might play a role in controlling the intracellular pyrophosphate pool; Belongs to the HAD-like hydrolase superfamily. PpaX family.
 
  
 0.461
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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