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
pepNPepN protein; Aminopeptidase with broad substrate specificity to several peptides. It has more affinity for oligopeptides than for dipeptides. It plays an essential role in the metabolism, it may be involved in nitrogen supply or protein turnover. (846 aa)    
Predicted Functional Partners:
pepXP
X-prolyl dipeptidyl aminopeptidase; Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline; Belongs to the peptidase S15 family.
 
   
 0.984
pepO
Peptidase family M13; High confidence in function and specificity.
 
   
 0.972
pepM
PepM protein; 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.
   
 
 0.970
pepT
Peptidase T; Cleaves the N-terminal amino acid of tripeptides. Has a broad specificity for tripeptides with no clear preference for a particular tripeptide. Tripeptides with proline in the second position are an exception and are not hydrolyzed. Does not hydrolyze dipeptides, tetrapeptides, or oligopeptides (By similarity).
      
 0.966
pepP
Metallopeptidase family M24; High confidence in function and specificity; Belongs to the peptidase M24B family.
  
 
 0.937
pepQ
Xaa-Pro dipeptidase; High confidence in function and specificity; Belongs to the peptidase M24B family.
  
 
 0.933
pepV
Dipeptidase; High confidence in function and specificity.
  
 
 0.932
pepC
PepC protein; Aminopeptidase C (EC 3.4.22.40) (Bleomycin hydrolase); High confidence in function and specificity; Belongs to the peptidase C1 family.
    
 0.931
pepF
PepF protein; Peptidase M3B, oligoendopeptidase F; High confidence in function and specificity.
      
 0.917
glyA
GlyA protein; 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.
    
 0.849
Your Current Organism:
Lactococcus lactis
NCBI taxonomy Id: 416870
Other names: L. lactis subsp. cremoris MG1363, Lactococcus lactis subsp. cremoris MG1363, Lactococcus lactis subsp. cremoris str. MG1363, Lactococcus lactis subsp. cremoris strain MG1363
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