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hslO protein (Pseudoflavonifractor capillosus) - STRING interaction network
"hslO" - Heat shock protein 33 homolog in Pseudoflavonifractor capillosus
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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
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textmining
co-expression
protein homology
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[Homology]
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hslOHeat shock protein 33 homolog ; 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 (291 aa)    
Predicted Functional Partners:
BACCAP_01193
Methyltransferase domain protein (249 aa)
 
          0.854
BACCAP_01192
TrpR family protein YerC/YecD (103 aa)
              0.800
BACCAP_02735
S4 domain protein (80 aa)
   
   
  0.694
BACCAP_00741
HAD hydrolase, TIGR02254 family (232 aa)
   
 
    0.610
BACCAP_03262
ATP-dependent zinc metalloprotease FtsH ; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins (665 aa)
   
   
  0.517
BACCAP_03249
ATP-dependent zinc metalloprotease FtsH ; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins (625 aa)
   
   
  0.517
BACCAP_01420
ATP-dependent zinc metalloprotease FtsH ; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins (764 aa)
   
   
  0.517
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, [...] (387 aa)
   
   
  0.515
BACCAP_02323
CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase (182 aa)
       
    0.500
BACCAP_04760
tRNA-dihydrouridine synthase ; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines (311 aa)
 
   
  0.498
Your Current Organism:
Pseudoflavonifractor capillosus
NCBI taxonomy Id: 411467
Other names: Bacillus capillosus, Bacteroides capillosus, Bacteroides capillosus ATCC 29799, P. capillosus, P. capillosus ATCC 29799, Pseudobacterium capillosum, Pseudoflavonifractor, Pseudoflavonifractor Carlier et al. 2010, Pseudoflavonifractor capillosus, Pseudoflavonifractor capillosus ATCC 29799, Pseudoflavonifractor capillosus str. ATCC 29799, Pseudoflavonifractor capillosus strain ATCC 29799, Ristella capillosa
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