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Mettu_1729 protein (Methylobacter tundripaludum) - STRING interaction network
"Mettu_1729" - Helix-turn-helix domain protein 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_1729Helix-turn-helix domain protein (92 aa)    
Predicted Functional Partners:
Mettu_1821
NAD+ synthetase (536 aa)
       
  0.886
Mettu_3837
Putative uncharacterized protein (91 aa)
   
          0.756
Mettu_1445
Putative uncharacterized protein (111 aa)
   
          0.694
atpH
F-type ATPase subunit delta ; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (176 aa)
       
      0.657
Mettu_0773
CinA domain protein (160 aa)
       
    0.523
Mettu_4071
Nucleoside recognition domain protein (409 aa)
   
          0.521
Mettu_3702
Long-chain-fatty-acid--(Acyl-carrier-protein) ligase., 6-deoxyerythronolide-B synthase (3566 aa)
         
  0.505
Mettu_3373
Hemerythrin-like metal-binding protein (131 aa)
   
          0.504
Mettu_3841
Acyl-(Acyl-carrier-protein)--phospholipid O-acyltransferase (713 aa)
         
  0.499
speD
S-adenosylmethionine decarboxylase proenzyme ; Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine (268 aa)
         
  0.496
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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