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Mettu_1605 protein (Methylobacter tundripaludum) - STRING interaction network
"Mettu_1605" - Protease Do in Methylobacter tundripaludum
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query proteins and first shell of interactors
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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
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
Mettu_1605Protease Do (456 aa)    
Predicted Functional Partners:
Mettu_1170
Protein serine/threonine phosphatase (578 aa)
   
  0.912
rpoH
RNA polymerase sigma-32 factor ; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is involved in regulation of expression of heat shock genes (285 aa)
   
 
  0.838
Mettu_4107
Peptidyl-prolyl cis-trans isomerase (160 aa)
     
 
  0.833
rpoS
Sigma-38 (342 aa)
   
 
  0.775
clpP
Endopeptidase Clp ; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (215 aa)
   
 
  0.741
dnaK
Heat shock protein 70 ; Acts as a chaperone (644 aa)
   
 
  0.727
rpoD
Sigma-70 ; 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 (602 aa)
   
 
  0.698
Mettu_2412
Carboxyl-terminal protease (437 aa)
   
   
  0.687
bamA
Outer membrane protein assembly factor BamA ; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane (793 aa)
   
   
  0.677
grpE
HSP-70 cofactor ; 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- depend [...] (203 aa)
     
   
  0.676
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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