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
ltaSCEnzyme responsible for polyglycerolphosphate LTA synthesis; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the LTA synthase family. (638 aa)    
Predicted Functional Partners:
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 [...]
  
  
 0.791
ypjQ
Putative phosphatidylglycerophosphatase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; To B.subtilis YutG.
   
  
 0.682
yceG
Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function.
      
 0.681
ytxK
Putative nucleic acid methyltransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; To type I restriction system adenine methylases.
  
     0.651
yqgQ
Putative single strand nucleic acid binding transcription factor; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pf: putative factor.
 
    0.650
yqgT
Putative gamma-D-glutamyl-L-diamino acid endopeptidase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the peptidase M14 family.
  
    0.630
glcK
Glucose kinase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the ROK (NagC/XylR) family.
  
    0.550
ygxA
Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function.
  
     0.529
yhzD
Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function.
  
     0.504
dagK
Diacylglycerol kinase; Catalyzes the phosphorylation of diacylglycerol (DAG) into phosphatidic acid. Is a key enzyme involved in the production of lipoteichoic acid by reintroducing DAG formed from the breakdown of membrane phospholipids into the phosphatidylglycerol biosynthetic pathway. Is more active toward long-chain DAG compared with short-chain DAG. Is not able to phosphorylate substrates other than DAG, such as monoacylglycerol, ceramide, undecaprenol, phosphatidylinositol, or sphingosine; Belongs to the diacylglycerol/lipid kinase family.
 
   
 0.499
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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