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hrcA protein (Methylobacter tundripaludum) - STRING interaction network
"hrcA" - Heat-inducible transcription repressor HrcA in Methylobacter tundripaludum
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
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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[Homology]
Score
hrcAHeat-inducible transcription repressor HrcA; Negative regulator of class I heat shock genes (grpE- dnaK-dnaJ and groELS operons). Prevents heat-shock induction of these operons (372 aa)    
Predicted Functional Partners:
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 [...] (203 aa)
   
   
  0.975
dnaK
Chaperone protein DnaK; Acts as a chaperone (644 aa)
   
   
  0.948
Mettu_3601
Heat shock protein 70; KEGG- sli-Slin_1429 DnaK-type molecular chaperone DnaK; manually curated; PFAM- Heat shock protein 70 (432 aa)
   
   
  0.826
Mettu_3235
KEGG- mca-MCA1305 DnaK-related protein; Belongs to the heat shock protein 70 family (646 aa)
   
   
  0.824
Mettu_0186
KEGG- nhl-Nhal_2957 putative chaperone heat-shock protein; Belongs to the heat shock protein 70 family (932 aa)
   
   
  0.824
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 [...] (376 aa)
   
   
  0.709
groL
60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (550 aa)
   
   
  0.676
groS
10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter (95 aa)
     
   
  0.656
Mettu_3921
PFAM- 3-hydroxyacyl-CoA dehydrogenase, NAD binding; 3-hydroxyacyl-CoA dehydrogenase, C-terminal; Crotonase, core; KEGG- rce-RC1_1947 3-hydroxyacyl-CoA dehydrogenase, putative (779 aa)
       
  0.647
birA
Bifunctional ligase/repressor BirA; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5’-adenylate (BirA-bio- 5’-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon (332 aa)
           
  0.625
Your Current Organism:
Methylobacter tundripaludum
NCBI taxonomy Id: 697282
Other names: M. tundripaludum SV96, Methylobacter sp. SV96, Methylobacter tundripaludum, Methylobacter tundripaludum DSM 17260, Methylobacter tundripaludum SV96, Methylobacter tundripaludum str. SV96, Methylobacter tundripaludum strain SV96
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