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
Lcho_1831KEGG: amr:AM1_A0167 hypothetical protein. (307 aa)    
Predicted Functional Partners:
htpG
Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity.
   
 0.906
grpE
GrpE 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. Several rounds of ATP-dependent i [...]
  
 0.875
groL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
  
 0.780
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 [...]
  
 0.735
Lcho_3179
PFAM: DnaJ central domain protein; heat shock protein DnaJ domain protein; chaperone DnaJ domain protein; KEGG: eba:ebA3490 hypothetical protein.
  
 0.735
Lcho_3374
PFAM: heat shock protein DnaJ domain protein; chaperone DnaJ domain protein; KEGG: tbd:Tbd_1431 putative heat shock protein, DnaJ family.
  
 0.735
groS
Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
  
 
 0.715
Lcho_1136
KEGG: rfr:Rfer_0499 hypothetical protein.
  
 0.707
Lcho_1541
KEGG: mca:MCA2189 cytochrome c family protein.
  
 0.707
Lcho_1542
TIGRFAM: cytochrome C family protein; KEGG: aba:Acid345_0471 hypothetical protein.
  
 0.707
Your Current Organism:
Leptothrix cholodnii
NCBI taxonomy Id: 395495
Other names: L. cholodnii SP-6, Leptothrix cholodnii SP-6, Leptothrix cholodnii str. SP-6, Leptothrix cholodnii strain SP-6
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