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
pepXXaa-Pro dipeptidyl-peptidase. Serine peptidase. MEROPS family S15; Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline; Belongs to the peptidase S15 family. (811 aa)    
Predicted Functional Partners:
LVIS_1783
Prolyl aminopeptidase; Releases the N-terminal proline from various substrates. Belongs to the peptidase S33 family.
 
   
 0.970
pip
Tricorn interacting factor F1. Serine peptidase. MEROPS family S33; Releases the N-terminal proline from various substrates.
 
   
 0.912
pepT
Peptidase T. Metallo peptidase. MEROPS family M20B; Cleaves the N-terminal amino acid of tripeptides. Belongs to the peptidase M20B family.
      
 0.881
LVIS_1756
Lysyl aminopeptidase. Metallo peptidase. MEROPS family M01.
 
   
 0.801
map
Methionine aminopeptidase, type I; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.
      
 0.757
map-2
Methionine aminopeptidase, type I; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.
      
 0.757
LVIS_0982
Aminopeptidase P; Belongs to the peptidase M24B family.
      
 0.682
LVIS_1781
Amino acid transporter.
  
    0.656
LVIS_0695
Hypothetical protein.
  
     0.648
LVIS_0572
Aminopeptidase C. Cysteine peptidase. MEROPS family C01B; Belongs to the peptidase C1 family.
     
 0.627
Your Current Organism:
Lactobacillus brevis
NCBI taxonomy Id: 387344
Other names: L. brevis ATCC 367, Lactobacillus brevis ATCC 367, Lactobacillus brevis str. ATCC 367, Lactobacillus brevis strain ATCC 367
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.