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
ampHD-alanyl-D-alanine- carboxypeptidase/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. Belongs to the beta-lactamase family. (385 aa)    
Predicted Functional Partners:
dacB
D-alanyl-D-alanine carboxypeptidase; Not involved in transpeptidation but exclusively catalyzes a DD-carboxypeptidase and DD-endopeptidase reaction. Belongs to the peptidase S13 family.
  
   
 0.868
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); In the N-terminal section; belongs to the glycosyltransferase 51 family.
     
 0.825
dacD
D-alanyl-D-alanine carboxypeptidase; Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors; Belongs to the peptidase S11 family.
      
 0.815
mepH
Murein DD-endopeptidase, space-maker hydrolase; A murein DD-endopeptidase with specificity for D-Ala-meso- diaminopimelic acid (mDAP) cross-links. Its role is probably to cleave D-Ala-mDAP cross-links to allow insertion of new glycans and thus cell wall expansion. Functionally redundant with MepM and MepH. Partially suppresses an mepS disruption mutant.
  
 
 0.800
pbpG
D-alanyl-D-alanine endopeptidase; Cell wall formation. May play a specialized role in remodeling the cell wall. Specifically hydrolyzes the DD- diaminopimelate-alanine bonds in high-molecular-mass murein sacculi; Belongs to the peptidase S11 family.
   
  
 0.795
dacA
D-alanyl-D-alanine carboxypeptidase (penicillin-binding protein 5); Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors.
   
  
 0.792
dacC
D-alanyl-D-alanine carboxypeptidase; Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors.
      
 0.792
mrcB
Fused glycosyl transferase 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); In the N-terminal section; belongs to the glycosyltransferase 51 family.
   
 
 0.769
pbpC
Penicillin-insensitive murein repair transglycosylase; Cell wall formation. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a transpeptidase C-terminal domain which may not be functional.
     
 0.761
mepS
Murein DD-endopeptidase MepS/Murein LD-carboxypeptidase; A murein DD-endopeptidase with specificity for D-Ala-meso- diaminopimelic acid (mDAP) cross-links. Its role is probably to cleave D-Ala-mDAP cross-links to allow insertion of new glycans and thus cell wall expansion. Functionally redundant with MepM and MepH. Also has weak LD-carboxypeptidase activity on L-mDAP-D-Ala peptide bonds. Partially suppresses a prc disruption mutant. Belongs to the peptidase C40 family.
  
 
 0.753
Your Current Organism:
Escherichia coli K12
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 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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