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Mettu_2386 protein (Methylobacter tundripaludum) - STRING interaction network
"Mettu_2386" - 33 kDa chaperonin in Methylobacter tundripaludum
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Known Interactions
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Predicted Interactions
gene neighborhood
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_2385
Putative uncharacterized protein (261 aa)
              0.834
Mettu_0046
Heat shock protein 15 (130 aa)
   
        0.773
hslU
Unfoldase 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)
     
   
  0.693
ribB
3,4-dihydroxy-2-butanone 4-phosphate synthase ; Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate (367 aa)
              0.678
Mettu_2387
Peptide-methionine (S)-S-oxide reductase ; 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)
         
  0.664
dusA
tRNA-dihydrouridine synthase A ; 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. Specifically modifies U20 and U20a in tRNAs (331 aa)
 
   
  0.645
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, [...] (376 aa)
     
   
  0.612
Mettu_1923
HAD-superfamily hydrolase, subfamily IA, variant 3 (218 aa)
   
 
    0.609
Mettu_3685
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 (650 aa)
   
   
  0.609
Mettu_3204
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 (647 aa)
   
   
  0.609
Your Current Organism:
Methylobacter tundripaludum
NCBI taxonomy Id: 697282
Other names: M. tundripaludum, M. tundripaludum SV96, Methylobacter, Methylobacter sp. SV96, Methylobacter tundripaludum, Methylobacter tundripaludum DSM 17260, Methylobacter tundripaludum SV96, Methylobacter tundripaludum Wartiainen et al. 2006, Methylobacter tundripaludum str. SV96, Methylobacter tundripaludum strain SV96
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