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:
some 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
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
ldtCL,d-transpeptidase linking lpp to murein; Responsible, at least in part, for anchoring of the major outer membrane lipoprotein (Lpp, also known as the Braun lipoprotein) to the peptidoglycan via a meso-diaminopimelyl-L-Lys- bond on the terminal residue of Lpp (320 aa)    
Predicted Functional Partners:
dacC
Serine-type d-ala-d-ala carboxypeptidase (penicillin-binding protein 5/6); Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors
    
 0.954
dacA
Serine-type d-ala-d-ala carboxypeptidase (penicillin-binding protein 5/6); Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors
    
 0.940
ampH
Peptidoglycan dd-carboxypeptidase/peptidoglycan dd-endopeptidase; Hydrolyzes the cross-linked dimers tetrapentapeptide (D45) and tetratetrapeptide (D44). Removes the terminal D-alanine from muropeptides and disaccharide pentapeptide M5 with a C-terminal D-Ala- D-Ala dipeptide. Associated with recycling and remodeling of peptidoglycan (PG). Also displays a low beta-lactamase activity
    
 0.930
mrcB
Peptidoglycan glycosyltransferase/peptidoglycan dd-transpeptidase mrcb; 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)
  
 
 0.927
dacD
Serine-type d-ala-d-ala carboxypeptidase (penicillin-binding protein 5/6); Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors
    
 0.921
ldtD
Murein l,d-transpeptidase; Responsible, at least in part, for generating a meso- diaminopimelyl-3-a meso-diaminopimelyl-3 cross-link
 
 
 
 0.913
mrcA
Penicillin-binding protein 1a, murein transglycosylase and transpeptidase; 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)
    
 0.912
yfeW
Serine-type d-ala-d-ala carboxypeptidase; Penicillin-binding protein. Has low DD-carboxypeptidase activity
    
 0.911
spy
An ATP-independent periplasmic chaperone, decreases protein aggregation and helps protein refolding. Binds substrate over a large region of its convex inner surface . Substrate protein folds while it is bound to chaperone . Increasing Spy flexibility increases its substrate affinity and overall chaperone activity (shown for 3 different substrates) . Protects proteins in vitro against tannin inactivation; tannins have antimicrobial activity . Overexpression enhances the stability of otherwise unstable periplasmic proteins
  
  
 0.847
yafK
annotation not available
 
  
 0.808
Your Current Organism:
Escherichia coli K12 MG1655
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli K12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
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