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
yvbXPutative epimerase modification of peptidoglycan; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the glycosyl hydrolase 18 family. (344 aa)    
Predicted Functional Partners:
ykvT
Cell wall hydrolase related to spore cortex-lytic enzymes; Evidence 2b: Function of strongly homologous gene; enzyme.
  
   
 0.981
ydaM
Putative glycosyltransferase associated to biofilm formation; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme.
     0.919
pdaC
N-acetylmuramic acid deacetylase; Catalyzes the deacetylation of N-acetylmuramic acid (MurNAc) residues in peptidoglycan, a modification that confers resistance to lysosyme. Is not able to deacetylate N-acetylglucosamine (GlcNAc) residues in peptidoglycan, but can deacylate chitin oligomers such as GlcNAc4 and GlcNAc5. Is essentially not active toward chitosan (partially deacetylated GlcNAc polymer) and has very low activity toward chitin (GlcNAc polymer). Does not deacetylate GlcNAc. In the N-terminal section; belongs to the RsiV family.
 
 
    0.900
pdaA
Exported N-acetylmuramic acid deacetylase; Catalyzes the deacetylation of N-acetylmuramic acid (MurNAc) residues in glycan strands of peptidoglycan, leading to the formation of muramic delta-lactam residues in spore cortex, after transpeptidation of deacetylated muramic acid residues. PdaA probably carries out both deacetylation and lactam ring formation and requires the product of CwlD activity on peptidoglycan as a substrate. Is required for germination. Cannot use chitin oligomer (hexa-N- acetylchitohexaose) as a substrate; Belongs to the polysaccharide deacetylase family.
 
      0.882
ypeB
Spore membrane component; Required for spore cortex hydrolysis during germination. Appears to be required for either expression, localization, activation or function of SleB.
      
 0.751
sleB
Spore cortex-lytic enzyme; Could be a lytic transglycosylase. Required for spore cortex hydrolysis during germination. Interacts strongly but noncovalently with spore components.
  
   
 0.725
cwlJ
Cell wall hydrolase; Probable spore cortex-lytic enzyme involved in the depolymerization of cortex peptidoglycan during germination.
      
 0.630
yheN
Putative polysaccharide deacetylase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme.
 
 
    0.629
ybaN
Polysaccharide deacetylase involved in sporulation; Necessary to maintain spores after the late stage of sporulation. Might be involved in cortex formation.
 
      0.569
lutB
Component of an iron-sulfur oxidase; Is essential for L-lactate degradation and allows cells to grow with lactate as the sole carbon source. Has probably a role as an electron transporter during oxidation of L-lactate. May also allow cells to utilize an alternative carbon source during biofilm formation, since it contributes to the formation of architecturally complex communities when lactate is present.
  
    0.521
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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