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Mettu_3542 protein (Methylobacter tundripaludum) - STRING interaction network
"Mettu_3542" - Tol-pal system protein YbgF in Methylobacter tundripaludum
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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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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_3542Tol-pal system protein YbgF (285 aa)    
Predicted Functional Partners:
Mettu_3543
Peptidoglycan-associated lipoprotein (191 aa)
 
        0.973
tolB
Protein TolB ; Involved in the TonB-independent uptake of proteins (427 aa)
 
   
  0.964
Mettu_3547
Protein TolQ (225 aa)
 
     
  0.891
queE
Queuosine biosynthesis protein QueE ; Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7- carboxy-7-deazaguanine (CDG), a step common to the biosynthetic pathways of all 7-deazapurine-containing compounds (213 aa)
              0.883
queC
Queuosine biosynthesis protein QueC ; Catalyzes the ATP-dependent conversion of 7-carboxy-7- deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)) (225 aa)
              0.883
Mettu_3546
Protein TolR (142 aa)
 
   
  0.798
Mettu_3548
Tol-pal system-associated acyl-CoA thioesterase (134 aa)
   
   
  0.719
Mettu_3552
Probable transcriptional regulatory protein Mettu_3552 (248 aa)
   
        0.678
ruvC
Holliday junction resolvase RuvC ; Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5’-terminal phosphate and a 3’-terminal hydroxyl group (165 aa)
              0.662
ruvA
Holliday junction ATP-dependent DNA helicase RuvA ; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB (203 aa)
              0.662
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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