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
SFP70808.1Oligopeptidase A Metallo peptidase. MEROPS family M03A. (699 aa)    
Predicted Functional Partners:
SFP70770.1
Hypothetical protein.
       0.804
SFP70836.1
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily.
 
     0.664
htpG
Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity.
  
  
 0.483
apaH
Bis(5'nucleosyl)-tetraphosphatase, ApaH; Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP; Belongs to the Ap4A hydrolase family.
  
  
 0.441
hslU
ATP-dependent HslUV protease ATP-binding subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.
  
  
 0.421
groL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
  
 
 0.420
groL-2
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
  
 
 0.420
pepA
Aminopeptidase A. Metallo peptidase. MEROPS family M17; Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N- terminal amino acids from various peptides.
   
  
 0.403
Your Current Organism:
Pseudomonas borbori
NCBI taxonomy Id: 289003
Other names: DSM 17834, LMG 23199, LMG:23199, P. borbori, Pseudomonas borbori Vanparys et al. 2006, Pseudomonas sp. R-20946, Pseudomonas sp. R-20955, Pseudomonas sp. R-23040, strain R-20821
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.