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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
KRN58399.1xaa-Pro dipeptidyl-peptidase; Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. (800 aa)    
Predicted Functional Partners:
KRN58400.1
Prolyl aminopeptidase; Releases the N-terminal proline from various substrates. Belongs to the peptidase S33 family.
 
   
 0.924
KRN59609.1
Peptidase M1 membrane alanine aminopeptidase.
 
   
 0.843
KRN58955.1
Prolyl aminopeptidase; Releases the N-terminal proline from various substrates. Belongs to the peptidase S33 family.
     
 0.754
pepT
Peptidase T; Cleaves the N-terminal amino acid of tripeptides. Belongs to the peptidase M20B family.
      
 0.744
KRN58517.1
Endothelin-converting protein 1.
      
 0.744
KRN59608.1
Bleomycin hydrolase; Belongs to the peptidase C1 family.
      
 0.744
KRN59121.1
Xaa-Pro dipeptidase; Belongs to the peptidase M24B family.
      
 0.743
map
Methionine aminopeptidase; 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.
      
 0.741
KRN59196.1
Dipeptidase PepV.
      
 0.738
KRN59508.1
Hypothetical protein.
  
     0.680
Your Current Organism:
Lactobacillus secaliphilus
NCBI taxonomy Id: 396268
Other names: CCUG 53218, DSM 17896, JCM 15613, L. secaliphilus, Lactobacillus secaliphilus Ehrmann et al. 2007
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.