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JG24_04635 protein (Klebsiella pneumoniae) - STRING interaction network
"JG24_04635" - FIG000875: Thioredoxin domain-containing protein EC-YbbN in Klebsiella pneumoniae
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second shell of interactors
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some 3D structure is known or predicted
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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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JG24_04635FIG000875- Thioredoxin domain-containing protein EC-YbbN; Derived by automated computational analysis using gene prediction method- Protein Homology (284 aa)    
Predicted Functional Partners:
gltB
Glutamate synthase [NADPH] large chain; Catalyzes the formation of glutamate from glutamine and alpha-ketoglutarate; Derived by automated computational analysis using gene prediction method- Protein Homology (1486 aa)
       
      0.854
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)
 
   
  0.766
htpG
Chaperone protein HtpG; Molecular chaperone. Has ATPase activity (624 aa)
   
 
  0.757
JG24_07085
Thioredoxin reductase; Catalyzes the transfer of electrons from NADPH to thioredoxin; FAD/NAD(P) binding; Derived by automated computational analysis using gene prediction method- Protein Homology; Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family (322 aa)
   
 
  0.732
hslU
ATP-dependent protease ATPase subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis (444 aa)
     
 
  0.722
JG24_04640
Putative NAD(P)-dependent oxidoreductase EC-YbbO; Derived by automated computational analysis using gene prediction method- Protein Homology; Belongs to the short-chain dehydrogenases/reductases (SDR) family (256 aa)
              0.675
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 (857 aa)
   
 
  0.671
dnaK
Chaperone protein DnaK; Acts as a chaperone (638 aa)
 
 
  0.669
JG24_29485
Chaperone protein DnaJ; Chaperone Hsp40; co-chaperone with DnaK; 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; Derived by automated computational analysis using gene prediction method- Protein Homology (377 aa)
   
 
  0.659
hslV
ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery (176 aa)
   
   
  0.637
Your Current Organism:
Klebsiella pneumoniae
NCBI taxonomy Id: 573
Other names: ATCC 13883, Bacillus pneumoniae, Bacterium pneumoniae crouposae, CCUG 225, CIP 82.91, DSM 30104, HAMBI 450, Hyalococcus pneumoniae, IFO 14940, K. pneumoniae, Klebsiella pneumoniae, Klebsiella sp. M-AI-2, Klebsiella sp. PB12, Klebsiella sp. RCE-7, LMG 2095, NBRC 14940, NCTC 9633
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