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
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
ybfMPutative membrane phosphatase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (162 aa)    
Predicted Functional Partners:
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.
  
  
 0.967
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.
  
  
 0.920
pbpX
Penicillin-binding endopeptidase X; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the beta-lactamase family.
      
 0.645
sigX
RNA polymerase ECF(extracytoplasmic function)-type sigma factor sigma(X); Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. May be involved in the regulation of iron metabolism; Belongs to the sigma-70 factor family. ECF subfamily.
   
  
 0.641
ybfN
Hypothetical protein; Evidence 5: No homology to any previously reported sequences.
       0.609
mprF
Phosphatidylglycerol lysyltransferase involved in lysinylation of phospholipids; Catalyzes the transfer of a lysyl group from L-lysyl- tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), one of the components of the bacterial membrane with a positive net charge. LPG synthesis contributes to the resistance to cationic antimicrobial peptides (CAMPs) and likely protects B.subtilis against its own CAMPs and against those produced by competiting microorganisms (bacteriocins). In fact, the modification of anionic phosphatidylglycerol with po [...]
  
  
 0.576
ybfK
Carboxylesterase NP; Shows carboxylesterase activity in vitro.
  
    0.490
yngC
Putative integral inner membrane protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pm: putative membrane component.
 
   
0.460
ybfO
Putative exported hydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme.
       0.416
dltA
D-alanine:D-alanyl-carrier protein ligase; Catalyzes the first step in the D-alanylation of lipoteichoic acid (LTA), the activation of D-alanine and its transfer onto the D- alanyl carrier protein (Dcp) DltC. In an ATP-dependent two-step reaction, forms a high energy D-alanyl-AMP intermediate, followed by transfer of the D-alanyl residue as a thiol ester to the phosphopantheinyl prosthetic group of the Dcp. D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net charge of the cell wall. Belongs to the ATP [...]
   
  
 0.408
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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