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
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
mtgAPeptidoglycan transglycosylase; Peptidoglycan polymerase that catalyzes glycan chain elongation from lipid-linked precursors; Belongs to the glycosyltransferase 51 family. (240 aa)    
Predicted Functional Partners:
mrdA
Penicillin-binding protein 2; Catalyzes cross-linking of the peptidoglycan cell wall. Belongs to the transpeptidase family. MrdA subfamily.
 
 
 0.974
ftsI2
Cell division protein FtsI; Catalyzes cross-linking of the peptidoglycan cell wall at the division septum.
 
 
 0.945
mrcA
Penicillin-binding protein 1A; Bifunctional murein transglycosylase/murein transpeptidase; penicillin-binding protein 1A; involved in the synthesis of cross-linked peptidoglycan from the lipid intermediates in cell wall formation; penicillin-insensitive transglycosylase catalyzes the formation of linear glycan strands and the penicillin-sensitive transpeptidase catalyzes the cross-linking of the peptide subunits; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
0.941
ftsI
Cell division protein FtsI; Catalyzes cross-linking of the peptidoglycan cell wall at the division septum; Belongs to the transpeptidase family. FtsI subfamily.
   
 0.937
mrcB
Bifunctional glycosyl transferase/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).
  
  
0.932
pbpC
Penicillin-binding protein 1C; Penicillin-insensitive transglycosylase/transpeptidase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 
0.911
dacA
D-alanyl-D-alanine carboxypeptidase; Penicillin-binding protein 5; removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase S11 family.
   
 
 0.911
dacC
D-alanyl-D-alanine carboxypeptidase; Penicillin-binding protein 5; removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase S11 family.
   
 
 0.911
elb2
Isoprenoid biosynthesis protein; Displays glyoxalase activity, catalyzing the conversion of glyoxal to glycolate; Belongs to the peptidase C56 family.
  
  
 0.910
dacB
D-alanyl-D-alanine carboxypeptidase; Penicillin binding protein 4; penicillin sensitive; catalyzes the formation of D-alanine from D-alanyl-D-alanine; one of four, DD-carboxypeptidase low-molecular weight penicillin-binding proteins that remove terminal D-alanine from pentapeptide side chains; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.910
Your Current Organism:
Yersinia ruckeri
NCBI taxonomy Id: 29486
Other names: ATCC 29473, CCM 6093, CCUG 14190, CDC 2396-61, CIP 82.80, DSM 18506, JCM 15110, JCM 2429, NCIB 2194, NCIMB 2194, NCTC 12986, Y. ruckeri
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