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
htpXHeat shock protein HtpX; Belongs to the peptidase M48B family. (302 aa)    
Predicted Functional Partners:
LIP_2724
Hypothetical protein.
 
     0.946
LIP_2721
Hypothetical protein.
 
     0.687
grpE
Co-chaperone GrpE; 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-depend [...]
  
  
 0.654
LIP_2722
Hypothetical protein.
       0.560
LIP_2729
Hypothetical protein.
 
     0.553
LIP_2730
Phage-shock protein.
 
    0.545
dnaJ
Molecular chaperone 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, [...]
  
 
 0.510
LIP_2725
Hypothetical protein.
       0.470
vapC-3
Hypothetical protein; Toxic component of a toxin-antitoxin (TA) system. An RNase. Belongs to the PINc/VapC protein family.
       0.470
LIP_1815
Microtubule-severing ATPase; Belongs to the AAA ATPase family.
  
 
 0.466
Your Current Organism:
Limnochorda pilosa
NCBI taxonomy Id: 1555112
Other names: DSM 28787, L. pilosa, Limnochorda pilosa Watanabe et al. 2015, NBRC 110152, bacterium HC45, strain HC45
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.