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.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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.
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experimentally determined
co-expression
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gene co-occurrence
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mltAMembrane-bound lytic murein transglycosylase A; Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division. (365 aa)    
Predicted Functional Partners:
slt
Soluble lytic murein transglycosylase; Murein-degrading enzyme. Catalyzes the cleavage of the glycosidic bonds between N-acetylmuramic acid and N-acetylglucosamine residues in peptidoglycan. May play a role in recycling of muropeptides during cell elongation and/or cell division (By similarity).
  
   
 0.895
mltB
Similar to E. coli membrane-bound lytic murein transglycosylase B (AAC75743.1); Blastp hit to AAC75743.1 (361 aa), 92% identity in aa 1 - 361.
  
  
 0.887
emtA
Membrane-bound lytic murein transglycosylase E; Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division. Preferentially cleaves at a distance of more than two disaccharide units from the ends of the glycan chain.
   
  
 0.798
mrcB
Transpeptidase of penicillin-binding protein 1b; Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross- linking of the peptide subunits).
   
 
 0.776
yfhD
Putative periplasmic amino acid binding protein; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family.
      
 0.761
mltC
Membrane-bound lytic murein transglycosylase C; Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division.
   
  
 0.751
yceG
Putative periplasmic solute-binding protein; Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation.
     
 0.733
rlpA
A minor lipoprotein; Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides; Belongs to the RlpA family.
  
   
 0.720
dacD
DD-carboxypeptidase; Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors; Belongs to the peptidase S11 family.
      
 0.679
ygdL
Similar to E. coli putative enzyme (AAC75854.1); Blastp hit to AAC75854.1 (268 aa), 93% identity in aa 1 - 267.
  
    0.631
Your Current Organism:
Salmonella enterica Typhimurium
NCBI taxonomy Id: 99287
Other names: S. enterica subsp. enterica serovar Typhimurium str. LT2, Salmonella enterica subsp. enterica serovar Typhimurium LT2, Salmonella enterica subsp. enterica serovar Typhimurium str. LT2, Salmonella enterica subsp. enterica serovar Typhimurium strain LT2, Salmonella enterica subsp. enterica serovar Typhimurium strain LT2-LTL2, Salmonella typhimurium LT2
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