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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Gene Fusion
Cooccurrence
Coexpression
Experiments
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[Homology]
Score
murQD-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. (304 aa)    
Predicted Functional Partners:
nagA
N-acetylglucosamine-6-phosphate deacetylase; Involved in the first committed step in the biosynthesis of amino-sugar-nucleotides. Catalyzes the hydrolysis of the N-acetyl group of N-acetylglucosamine-6-phosphate (GlcNAc-6-P) to yield glucosamine 6- phosphate and acetate; Belongs to the metallo-dependent hydrolases superfamily. NagA family.
 
 0.995
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.
 
  
 0.993
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.
  
 0.981
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.
 
  
 0.981
nagP
Phosphotransferase system (PTS) N-acetylglucosamine-specific enzyme IICB component; 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. This system is involved in N-acetylglucosamine transport (By similarity).
  
 
 0.939
ypqE
Putative phosphotransferase system enzyme IIA component; 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.
    
 0.921
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.
  
 0.917
yyzE
Putative phosphotransferase system enzyme IIA component; The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane.
    
 0.917
ybbC
Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function.
 
  
 0.882
ywpJ
Putative phosphatase; Catalyzes the dephosphorylation of phosphorylated 5-6 carbon sugars and monophosphate nucleotides (NMP) in vitro (By similarity). To a lesser extent, dephosphorylates flavin mononucleotide (FMN) in vitro.
      
 0.830
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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