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
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[Homology]
Score
nagZN-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. (642 aa)    
Predicted Functional Partners:
ybbC
Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function.
  
 0.999
amiE
Amidase hydrolyzing N-acetylmuramyl-L-Ala bond of MurNAc peptides; Involved in muropeptide recycling. Hydrolyzes the amide bond between N-acetylmuramic acid (MurNAc) and the L-alanine residue of the stem peptide. Cannot hydrolyze muropeptides containing N- acetylglucosamine (GlcNAc) at the non-reducing end.
  
 0.999
murQ
D-lactyl ether N-acetylmuramic-6-phosphate acid etherase; Specifically catalyzes the cleavage of the D-lactyl ether substituent of MurNAc 6-phosphate, producing GlcNAc 6-phosphate and D- lactate.
 
  
 0.994
ybbH
Putative transcriptional regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator.
 
  
 0.932
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.
     
 0.868
pepA
Leucyl aminopeptidase; Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N- terminal amino acids from various peptides (By similarity).
    
 0.852
ldcA
Muropeptide L,D-carboxypeptidase; May be involved in the degradation of peptidoglycan by catalyzing the cleavage of the terminal D-alanine residue from cytoplasmic murein peptides; Belongs to the peptidase S66 family.
  
 0.831
ybbF
Putative PTS system EIIBC component ybbF; The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane.
  
  
 0.802
lytG
Exoglucosaminidase; Is the major glucosaminidase responsible for peptidoglycan structural determination during vegetative growth. Catalyzes the hydrolysis of 1,4-beta-linkages between N-acetyl-D-glucosamine and N- acetylmuramic acid residues in peptidoglycan. Acts processively from the ends of the glycan strands. Also plays a role in motility, chemotaxis and cell division.
     
 0.763
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.
  
  
 0.734
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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