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
dacAD-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. (443 aa)    
Predicted Functional Partners:
ponA
Peptidoglycan glycosyltransferase (penicillin-binding proteins 1A and 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).
 
 
 0.987
dacC
D-alanyl-D-alanine carboxypeptidase; Catalyzes DD-carboxypeptidase and transpeptidation reactions.
     
 0.978
dacB
D-alanyl-D-alanine carboxypeptidase (penicillin-binding protein 5*); Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors. Required specifically for the synthesis of the spore form of peptidoglycan (cortex).
 
  
0.949
pbpC
Penicillin-binding lipoprotein 3; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type lp: lipoprotein.
 
  
 0.935
pbpF
Penicillin-binding protein 2C required for spore germination; Cell wall formation. May be involved in outgrowth of the germinated spore or it could function in the synthesis of the germ cell wall; In the N-terminal section; belongs to the glycosyltransferase 51 family.
  
 
 0.932
dacF
D-alanyl-D-alanine carboxypeptidase (penicilin binding protein); Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors.
  
  
0.925
yodJ
D-alanyl-D-alanine carboxypeptidase lipoprotein; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme.
   
 
 0.914
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.
     
 0.906
mreB
Cell-shape determining protein; Forms membrane-associated dynamic filaments that are essential for cell shape determination. Acts by regulating cell wall synthesis and cell elongation, and thus cell shape. A feedback loop between cell geometry and MreB localization may maintain elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature (By similarity). Filaments rotate around the cell circumference in concert with the cell wall synthesis enzymes. The process is driven by the cell wall synthesis machinery and does not depend on MreB polymerization. The [...]
 
  
 0.892
pbpD
Penicillin-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.
  
  
 0.851
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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