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
ACH52_0959Cell surface protein with subtilisin family serine protease domain protein. (1081 aa)    
Predicted Functional Partners:
ACH52_0960
Transglutaminase domain-containing protein.
  
    0.513
ACH52_0961
Xaa-His dipeptidase PepD.
     
 0.483
ACH52_0213
Type VII secretion protein EssC.
  
 
 0.441
ACH52_0325
M6 family metalloprotease domain-containing protein.
 
  
 0.438
ACH52_0958
Cell surface protein with subtilisin family serine protease domain protein; Belongs to the peptidase S8 family.
 
    
0.426
ACH52_0211
Serine/threonine protein kinase.
 
  
 0.425
ACH52_0232
FHA domain-containing protein.
 
 
 0.417
ACH52_0368
Hypothetical protein.
  
 
 0.405
secY
Preprotein translocase subunit SecY; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
    
 
 0.405
ACH52_0871
Cell surface protein.
  
 
 0.405
Your Current Organism:
Eubacterium limosum
NCBI taxonomy Id: 1736
Other names: ATCC 8486, Bacteroides limosus, Butyribacterium limosum, Butyribacterium rettgeri, CCUG 16793, CIP 104169, DSM 20543, E. limosum, JCM 6421, JCM 9978, Mycobacterium limosum
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