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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
dacCPenicillin-binding protein; Belongs to the peptidase S11 family. (419 aa)    
Predicted Functional Partners:
ftsI
Penicillin-binding protein; Catalyzes cross-linking of the peptidoglycan cell wall at the division septum.
 
 
 0.935
mrdA
Penicillin-binding protein; Catalyzes cross-linking of the peptidoglycan cell wall. Belongs to the transpeptidase family. MrdA subfamily.
  
 
 0.935
mtgA
Monofunctional biosynthetic peptidoglycan transglycosylase; Peptidoglycan polymerase that catalyzes glycan chain elongation from lipid-linked precursors; Belongs to the glycosyltransferase 51 family.
  
 
 0.915
BAV0846
Probable D-alanyl-D-alanine carboxypeptidase.
     
 0.912
BAV0072
Penicillin-binding protein 1A.
     
 0.907
mrcA
Penicillin-binding protein.
     
 0.907
pbpC
Penicillin-binding protein 1C.
     
 0.902
BAV0134
Conserved hypothetical protein.
 
     0.781
BAV0699
Putative transporter.
  
  
 0.713
lipB
Lipoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
 
    0.657
Your Current Organism:
Bordetella avium
NCBI taxonomy Id: 360910
Other names: B. avium 197N, Bordetella avium 197N, Bordetella avium str. 197N, Bordetella avium strain 197N
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