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
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[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.
 
 
 0.951
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.
 
 
 0.903
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.
  
 
 
 0.878
ftsW
Cell-division protein; Peptidoglycan polymerase that is essential for cell division.
  
 
 0.865
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.
  
  
 0.851
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.
 
 
 0.802
yuxK
Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; Belongs to the DCC thiol-disulfide oxidoreductase family.
  
    0.779
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.
   
 
 0.778
tagO
UDP-N-acetylglucosamine:undecaprenyl-P N-acetylglucosaminyl-1-P transferase; Catalyzes the formation of undecaprenyl-PP-N- acetylglucosamine. Involved in the synthesis of anionic cell-wall polymers as it mediates the initiation of the linkage unit formation that appears to be common to the two types of teichoic acids attached to the peptidoglycan of B.subtilis; may also be involved in teichuronic acid biosynthesis (Probable); Belongs to the glycosyltransferase 4 family.
  
  
 0.774
dacC
D-alanyl-D-alanine carboxypeptidase; Catalyzes DD-carboxypeptidase and transpeptidation reactions.
      
 0.721
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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