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
ldtAL,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 (310 aa)    
Predicted Functional Partners:
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
     
 0.939
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
     
 0.928
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
     
 0.916
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)
     
 0.910
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
     
 0.908
yfeW
Serine-type d-ala-d-ala carboxypeptidase; Penicillin-binding protein. Has low DD-carboxypeptidase activity
     
 0.903
yafK
annotation not available
 
   
 0.902
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)
     
 0.901
ldtD
Murein l,d-transpeptidase; Responsible, at least in part, for generating a meso- diaminopimelyl-3-a meso-diaminopimelyl-3 cross-link
 
   
 0.898
lpp
An outer membrane lipoprotein that controls the distance between the inner and outer membranes; adding residues to Lpp increases the width of the periplasm . The only protein known to be covalently linked to the peptidoglycan network (PGN) . Also non-covalently binds the PGN . The link between the cell outer membrane and PGN contributes to the maintenance of the structural and functional integrity of the cell envelope, and maintains the correct distance between the PGN and the outer membrane The most adundant cellular protein, there can be up to 10(6) Lpp molecules per cell . About one [...]
  
   
 0.721
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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