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JT27_18675 protein (Alcaligenes faecalis) - STRING interaction network
"JT27_18675" - Crystallin in Alcaligenes faecalis
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second shell of interactors
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proteins of unknown 3D structure
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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[Homology]
Score
JT27_18675Crystallin; Derived by automated computational analysis using gene prediction method- Protein Homology; Belongs to the small heat shock protein (HSP20) family (149 aa)    
Predicted Functional Partners:
htpG
Chaperone protein HtpG; Molecular chaperone. Has ATPase activity (634 aa)
   
 
  0.790
clpB
Chaperone protein ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family (863 aa)
   
 
  0.731
clpA
Clp protease ClpX; ATPase and specificity subunit of the ClpA-ClpP ATP dependent serine protease; directs protease to specific substrates; Derived by automated computational analysis using gene prediction method- Protein Homology; Belongs to the ClpA/ClpB family (773 aa)
   
 
  0.731
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 [...] (377 aa)
   
 
  0.729
dnaK
Chaperone protein DnaK; Acts as a chaperone (641 aa)
   
 
  0.725
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- dependent [...] (196 aa)
   
   
  0.614
groS
10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter (95 aa)
   
   
  0.596
JT27_16710
Quinone oxidoreductase; Derived by automated computational analysis using gene prediction method- Protein Homology (328 aa)
     
   
  0.577
JT27_05205
Quinone oxidoreductase; Derived by automated computational analysis using gene prediction method- Protein Homology (333 aa)
     
   
  0.577
groEL
60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (548 aa)
   
   
  0.573
Your Current Organism:
Alcaligenes faecalis
NCBI taxonomy Id: 511
Other names: A. faecalis, ATCC 8750, Alcaligenes faecalis, Alcaligenes sp. BP11, CIP 55.84, CIP 60.80, DSM 30030, IAM 12369, IFO 13111, JCM 20522, JCM 20663, NBRC 13111, NCAIM B.01104, NCIMB 8156, NCTC 11953
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