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
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Cooccurrence
Coexpression
Experiments
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Textmining
[Homology]
Score
groLHeat shock protein (groEL); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) family. (544 aa)    
Predicted Functional Partners:
dnaK
Heat shock protein 70 (dnaK); Acts as a chaperone; Belongs to the heat shock protein 70 family.
  
 0.997
groS
Chaperonin (groES); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
 
 
 0.997
grpE
grpE protein (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-depe [...]
  
 0.994
htpG
Heat shock protein 90 (htpG); Molecular chaperone. Has ATPase activity.
   
 0.989
lon
ATP-dependent protease LA (lon-2); ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
  
 
 0.974
TP_0098
Heat-shock protein, putative; Similar to PID:1046215 SP:P50025 percent identity: 45.69; identified by sequence similarity; putative.
  
 0.951
trxA
Thioredoxin (trx); Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.
  
 
 0.934
TP_0563
Predicted coding region TP0563; Hypothetical protein; identified by Glimmer; putative.
  
 0.926
TP_0939
Pyruvate oxidoreductase; Similar to PID:1001780 SP:P52965 PID:1006618 percent identity: 58.44; identified by sequence similarity; putative.
  
 
 0.886
fliY
Flagellar motor switch protein (fliY); FliN is one of three proteins (FliG, FliN, FliM) that form the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation. Belongs to the FliN/MopA/SpaO family.
   
   0.876
Your Current Organism:
Treponema pallidum
NCBI taxonomy Id: 243276
Other names: T. pallidum subsp. pallidum str. Nichols, Treponema pallidum Nichols, Treponema pallidum subsp. pallidum str. Nichols
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