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Mettu_2386 protein (Methylobacter tundripaludum) - STRING interaction network
"Mettu_2386" - 33 kDa chaperonin in Methylobacter tundripaludum
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second shell of interactors
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Known Interactions
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experimentally determined
Predicted Interactions
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gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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Mettu_238633 kDa chaperonin; 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 (289 aa)    
Predicted Functional Partners:
Mettu_0046
KEGG- mca-MCA1817 heat shock protein 15; PFAM- RNA-binding S4; SMART- RNA-binding S4; Belongs to the HSP15 family (130 aa)
   
   
  0.853
Mettu_2385
KEGG- mca-MCA1710 hypothetical protein (261 aa)
              0.839
Mettu_2484
KEGG- alv-Alvin_2848 sigma 54 modulation protein/ribosomal protein S30EA; TIGRFAM- Ribosomal protein S30Ae/sigma 54 modulation protein; PFAM- Ribosomal protein S30Ae/sigma 54 modulation protein (96 aa)
   
 
      0.725
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 (439 aa)
     
   
  0.725
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)
     
   
  0.723
hslV
ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery (182 aa)
   
   
  0.696
Mettu_2387
Peptide methionine sulfoxide reductase MsrA; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine (209 aa)
         
  0.672
htpG
Chaperone protein HtpG; Molecular chaperone. Has ATPase activity (642 aa)
   
   
  0.627
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)
     
   
  0.582
Mettu_2738
Cold-shock DNA-binding protein; KEGG- nwa-Nwat_0698 ribosomal subunit interface protein; PFAM- Cold-shock protein, DNA-binding; SMART- Cold shock protein (180 aa)
       
      0.578
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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