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
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.
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from curated databases
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experimentally determined
co-expression
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gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
pbpDPenicillin-binding protein 4; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; In the C-terminal section; belongs to the transpeptidase family. (624 aa)    
Predicted Functional Partners:
pbpC
Penicillin-binding lipoprotein 3; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type lp: lipoprotein.
 
 
 0.955
pbpB
Penicillin-binding protein 2B; Penicillin-binding proteins (PBPs) function in the late steps of murein biosynthesis. PBP-2B is required for vegetative cell division and sporulation septation. Beta-lactamase inactivates the PBPs by acylating an essential serine residue in the active site of these proteins, thereby interrupting normal cell wall synthesis; Belongs to the transpeptidase family.
 
 
 0.950
rodA
Factor involved in extension of the lateral walls of the cell; Peptidoglycan polymerase that is essential for cell wall elongation. Also required for the maintenance of the rod cell shape. Belongs to the SEDS family. MrdB/RodA subfamily.
  
 
 
 0.923
ftsW
Cell-division protein; Peptidoglycan polymerase that is essential for cell division.
  
 
 0.909
pbpH
Penicillin-binding enzyme for formation of rod-shaped peptidoglycan cell wall; Involved in the polymerization of peptidoglycan. Plays a redundant role with PBP2a in determining the rod shape of the cell during vegetative growth and spore outgrowth. Belongs to the transpeptidase family.
 
 
 0.846
dacA
D-alanyl-D-alanine carboxypeptidase (penicillin-binding protein 5); Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors; Belongs to the peptidase S11 family.
   
  
 0.809
yuxK
Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; Belongs to the DCC thiol-disulfide oxidoreductase family.
  
    0.798
mecA
Adaptor protein controlling oligomerization of the AAA+ protein ClpC; Enables the recognition and targeting of unfolded and aggregated proteins to the ClpC protease or to other proteins involved in proteolysis. Acts negatively in the development of competence by binding ComK and recruiting it to the ClpCP protease. When overexpressed, inhibits sporulation. Also involved in Spx degradation by ClpC.
      
 0.777
cwlC
N-acetylmuramoyl-L-alanine amidase; Autolysins are 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. CwlC is able to hydrolyze type A cell walls such as B.subtilis. Its main function is to lyze the mother cell wall peptidoglycan, playing a role during sporulation. Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.
   
 
 0.753
ftsZ
Cell-division initiation protein; Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity.
  
  
 0.749
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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