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
AQG74041.1Dipeptidase PepV; Divalent metal ion-dependent extracellular dipeptidase; able to hydrolyze a broad range of dipeptides but no tri-, tetra-, or larger oligopeptides; differences in the amino acid specificity of the cleavage site varies between species; similar to succinyl-diaminopimelate desuccinylases; Derived by automated computational analysis using gene prediction method: Protein Homology. (467 aa)    
Predicted Functional Partners:
AQG73829.1
Peptidase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.904
dapF
Diaminopimelate epimerase; Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L- lysine and an essential component of the bacterial peptidoglycan.
    
 0.820
AWJ15_10865
Acetyltransferase; Catalyzes the conversion of N-acetyl-diaminopimelate to diaminopimelate and acetate.
    
 0.795
glyA
Serine hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
    
 0.767
glmS
Glutamine--fructose-6-phosphate aminotransferase; Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
   
 
 0.668
AQG73681.1
Peptidase T; Cleaves the N-terminal amino acid of tripeptides. Belongs to the peptidase M20B family.
    
 0.645
argG
Argininosuccinate synthase; Catalyzes the formation of 2-N(omega)-(L-arginino)succinate from L-citrulline and L-aspartate in arginine biosynthesis, AMP-forming; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the argininosuccinate synthase family. Type 1 subfamily.
  
 0.622
AQG72930.1
Alanine racemase; Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids; Belongs to the alanine racemase family.
   
 
 0.604
ddl
D-alanine--D-alanine ligase; Cell wall formation; Belongs to the D-alanine--D-alanine ligase family.
     
 0.568
pyrC
Dihydroorotase; Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate; Belongs to the metallo-dependent hydrolases superfamily. DHOase family. Class I DHOase subfamily.
  
 
 0.563
Your Current Organism:
Lactobacillus rhamnosus
NCBI taxonomy Id: 47715
Other names: ATCC 7469, CCUG 21452, CIP A157, DSM 20021, IFO 3425, L. rhamnosus, LMG 6400, LMG:6400, Lactobacillus casei rhamnosus, Lactobacillus casei subsp. rhamnosus, Lactobacillus sp. NCIM 2587, Lactobacillus sp. W6, Lactobacillus sp. X9, NBRC 3425, NCAIM B.01147, NCCB 46033, NCDO 243, NCIB 6375, NCIMB 6375, NCTC 12953, NCTC 13764, NRRL B-442, VKM B-574
Server load: low (12%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.