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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
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[Homology]
Score
AGB30408.1Hypothetical protein. (358 aa)    
Predicted Functional Partners:
grpE
Molecular chaperone GrpE (heat shock protein); Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. [...]
  
  
 0.579
egsA
Glycerol dehydrogenase-like oxidoreductase; Catalyzes the NAD(P)H-dependent reduction of dihydroxyacetonephosphate (DHAP or glycerone phosphate) to glycerol 1- phosphate (G1P). The G1P thus generated is used as the glycerophosphate backbone of phospholipids in the cellular membranes of Archaea. Belongs to the glycerol-1-phosphate dehydrogenase family.
     
 0.562
AGB32165.1
DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain.
  
 
 0.476
AGB31890.1
DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain.
  
 
 0.470
dnaJ
Chaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, D [...]
  
 
 0.470
dnaK
Chaperone protein DnaK; Acts as a chaperone.
  
 
 0.454
AGB32731.1
Lon-related putative ATP-dependent protease; PFAM: Magnesium chelatase, subunit ChlI; Sigma-54 interaction domain; Lon protease (S16) C-terminal proteolytic domain; TIGRFAM: lon-related putative ATP-dependent protease; Belongs to the peptidase S16 family.
   
 
 0.402
AGB32992.1
Lon-related putative ATP-dependent protease; PFAM: Magnesium chelatase, subunit ChlI; Sigma-54 interaction domain; Lon protease (S16) C-terminal proteolytic domain; TIGRFAM: lon-related putative ATP-dependent protease; Belongs to the peptidase S16 family.
   
 
 0.402
Your Current Organism:
Natrinema pellirubrum
NCBI taxonomy Id: 797303
Other names: N. pellirubrum DSM 15624, Natrinema pellirubrum DSM 15624, Natrinema pellirubrum JCM 10476, Natrinema pellirubrum NCIMB 786, Natrinema pellirubrum str. DSM 15624, Natrinema pellirubrum strain DSM 15624
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