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BADO_0041 protein (Bifidobacterium adolescentis) - STRING interaction network
"BADO_0041" - annotation not available in Bifidobacterium adolescentis
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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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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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 each other.
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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Neighborhood
Gene Fusion
Cooccurence
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[Homology]
Score
BADO_0041annotation not available (153 aa)    
Predicted Functional Partners:
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 (905 aa)
   
 
  0.727
BADO_0586
annotation not available (864 aa)
   
 
  0.727
dnaK
Chaperone protein DnaK; Acts as a chaperone (627 aa)
   
 
  0.688
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 [...] (228 aa)
 
   
  0.655
nnrD
ADP-dependent (S)-NAD(P)H-hydrate dehydratase; Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration (591 aa)
 
        0.584
groS
10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter (97 aa)
   
   
  0.582
groL
60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (538 aa)
   
   
  0.573
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5’-3’ exonuclease activity (948 aa)
     
   
  0.561
sigA
RNA polymerase sigma factor SigA; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the primary sigma factor during exponential growth (478 aa)
     
   
  0.519
Your Current Organism:
Bifidobacterium adolescentis
NCBI taxonomy Id: 1680
Other names: AS 1.2190, ATCC 15703, B. adolescentis, BCRC 14606, Bifidobacterium adolescentis, CCRC 14606, CCUG 17359, CCUG 18363, CIP 64.59, DSM 20083, LMG 10502, NCAIM B.01822, NCTC 11814
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