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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Cooccurrence
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[Homology]
Score
lytCPutative undecaprenyl-phosphate N-acetylgalactosaminyl-1-phosphate transferase; Autolysins are cell wall hydrolases involved in some important biological processes such as cell separation, cell-wall turnover, competence for genetic transformation, formation of the flagella - in particular of its basal body - and sporulation. Has a high affinity for teichoic acid-endowed peptidoglycan. LytC is required for efficient swarming motility but not at the level of cell separation or flagellum biosynthesis. Rather, LytC appears to be important for proper flagellar function. (496 aa)    
Predicted Functional Partners:
lytA
Membrane bound lipoprotein; Possible role in the secretion of LytB and LytC.
  
  
 0.997
lytD
Exported N-acetylglucosaminidase (major autolysin) (CWBP90); Cell wall hydrolase not involved in cell autolysis, competence, sporulation or germination. It hydrolyzes the beta-1,4 glycan bond between the N-acetylglucosaminyl and the N-acetylmuramoyl residues in the glycan chain.
 
  
 0.988
lytF
gamma-D-glutamate-meso-diaminopimelate muropeptidase (major autolysin); Cell wall hydrolase that cleaves gamma-D-glutamate-meso- diaminopimelate bonds in peptidoglycan. LytF is necessary and sufficient for vegetative daughter cell separation, and also seems to play a role in cell autolysis.
 
  
 0.970
lytB
Modifier protein of major autolysin LytC; Possibly involved in cell wall metabolism during spore formation. Enhances the amidase activity approximately threefold.
 
  
0.957
lytE
Cell wall hydrolase; Cell wall hydrolase that cleaves gamma-D-glutamate-meso- diaminopimelate bonds in peptidoglycan (By similarity). Seems to play a role in cell separation during vegetative growth.
 
  
 0.943
yngK
Putative exported protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure.
    
 0.889
sigD
RNA polymerase sigma-28 factor (sigma-D); Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This alternative sigma factor is required for the transcription of the flagellin and motility genes as well as for wild- type chemotaxis.
   
  
 0.826
nagZ
N-acetylglucosaminidase lipoprotein; Plays a role in peptidoglycan recycling by cleaving the terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide- linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N- acetylmuramic acid and anhydro-N-acetylmuramic acid-linked peptides. Cleaves muropeptides, but not peptidoglycan. Belongs to the glycosyl hydrolase 3 family.
    
 0.777
lytH
Sporulation-specific L-Ala-D-Glu endopeptidase; L-Ala--D-Glu endopeptidase involved in production of single L-alanine side chains from tetrapeptides in the spore cortex peptidoglycan. Therefore, is required for the endospore cortex maturation.
  
  
 0.774
cwlO
Secreted cell wall DL-endopeptidase; The C-terminal part of CwlO shows a cell wall hydrolytic DL- endopeptidase activity; Belongs to the peptidase C40 family.
  
  
 0.702
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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