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
aroHPhospho-2-dehydro-3-deoxyheptonate aldolase; Phosphoenolpyruvate + D-Erythrose 4-phosphate + H2O <=> 2-Dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + Orthophosphate; Belongs to the class-II DAHP synthase family. (461 aa)    
Predicted Functional Partners:
aroB
3-dehydroquinate synthase / shikimate kinase, bifunctionnal enzyme; Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ); Belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family.
 
  
 0.954
CBL56181.1
Chorismate mutase EC:5.4.99.5 catalyses the conversion of chorismate to prephenate in the pathway of tyrosine and phenylalanine biosynthesis. This enzyme is negatively regulated by tyrosine, tryptophan and phenylalanine.
   
 
 0.901
rplV
50S ribosomal protein L22; The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome.
      
 0.708
nirA2/sir2
Sulfite reductase [ferredoxin]; Hydrogen sulfide + 6 oxidized ferredoxin + 3 H2O = sulfite + 6 reduced ferredoxin + 6 H+.Binds 1 siroheme per subunit Binds 1 4Fe-4S cluster per subunit; Belongs to the nitrite and sulfite reductase 4Fe-4S domain family.
      
 0.705
rpsG
30S ribosomal protein S7; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA; Belongs to the universal ribosomal protein uS7 family.
      
 0.704
rplC
50S ribosomal protein L3; One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit; Belongs to the universal ribosomal protein uL3 family.
      
 0.702
rplT
50S ribosomal protein L20; Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit.
      
 0.702
rplB
50S ribosomal protein L2; One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome. Belongs to the universal ribosomal protein uL2 family.
      
 0.673
plsC3
Smart00563, Phosphate acyltransferases; Function in phospholipid biosynthesis and have either glycerolphosphate, 1-acylglycerolphosphate, or 2-acylglycerolphosphoethanolamine acyltransferase activities.
       0.627
CBL57069.1
Zn-dependent hydrolase, beta-lactamase fold.
       0.563
Your Current Organism:
Propionibacterium freudenreichii
NCBI taxonomy Id: 754252
Other names: P. freudenreichii subsp. shermanii CIRM-BIA1, Propionibacterium freudenreichii subsp. shermanii ATCC 9614, Propionibacterium freudenreichii subsp. shermanii CIP 103027, Propionibacterium freudenreichii subsp. shermanii CIRM-BIA1, Propionibacterium freudenreichii subsp. shermanii str. CIRM-BIA1, Propionibacterium freudenreichii subsp. shermanii strain CIRM-BIA1
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