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query proteins and first shell of interactors
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proteins of unknown 3D structure
filled nodes:
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EAQ23394.1Chaperonin, 33 kDa; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. (331 aa)    
Predicted Functional Partners:
EAQ22809.1
S4 domain protein; COG1188 Ribosome-associated heat shock protein implicated in the recycling of the 50S subunit (S4 paralog).
  
  
 0.898
EAQ23396.1
COG0617 tRNA nucleotidyltransferase/poly(A) polymerase; Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family.
 
    0.877
EAQ23397.1
23S rRNA (Uracil-5-)-methyltransferase rumA; COG2265 SAM-dependent methyltransferases related to tRNA (uracil-5-)-methyltransferase; Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family.
 
     0.877
hslU
ATP-dependent protease ATP-binding subunit; 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.
   
  
 0.828
EAQ23395.1
Putative phosphohydrolase (mutT/nudix family protein); COG0494 NTP pyrophosphohydrolases including oxidative damage repair enzymes.
  
    0.826
hslV
ATP-dependent protease peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
  
  
 0.795
EAQ23393.1
Hydrolase, NUDIX family protein; COG0494 NTP pyrophosphohydrolases including oxidative damage repair enzymes; Belongs to the Nudix hydrolase family.
 
     0.735
lon
ATP-dependent protease La; 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.
  
  
 0.718
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 [...]
  
  
 0.688
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 [...]
   
  
 0.633
Your Current Organism:
Roseovarius sp. 217
NCBI taxonomy Id: 314264
Other names: R. sp. 217
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