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Mettu_2537 protein (Methylobacter tundripaludum) - STRING interaction network
"Mettu_2537" - KEGG: mca:MCA2797 carbonic anhydrase 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
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[Homology]
Score
Mettu_2537KEGG- mca-MCA2797 carbonic anhydrase (178 aa)    
Predicted Functional Partners:
Mettu_0443
Phosphoenolpyruvate synthase; Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate; Belongs to the PEP-utilizing enzyme family (803 aa)
   
 
  0.766
Mettu_2536
PFAM- Permease YjgP/YjgQ, predicted; KEGG- mca-MCA2101 hypothetical protein; overlaps another CDS with the same product name (357 aa)
              0.663
Mettu_2535
PFAM- Permease YjgP/YjgQ, predicted; KEGG- mca-MCA2100 hypothetical protein; overlaps another CDS with the same product name (383 aa)
              0.663
Mettu_1889
Carbonic anhydrase; Reversible hydration of carbon dioxide (213 aa)
     
 
  0.658
Mettu_2600
KEGG- mca-MCA1695 cell division protein FtsK, putative; PFAM- Cell divisionFtsK/SpoIIIE; DNA translocase ftsK gamma; SMART- ATPase, AAA+ type, core (759 aa)
            0.656
Mettu_3832
Carbonic anhydrase; Reversible hydration of carbon dioxide (194 aa)
       
 
  0.646
Mettu_3921
PFAM- 3-hydroxyacyl-CoA dehydrogenase, NAD binding; 3-hydroxyacyl-CoA dehydrogenase, C-terminal; Crotonase, core; KEGG- rce-RC1_1947 3-hydroxyacyl-CoA dehydrogenase, putative (779 aa)
   
   
  0.609
Mettu_3360
TIGRFAM- Thioredoxin; KEGG- slt-Slit_2205 thioredoxin; PFAM- Thioredoxin domain (143 aa)
       
      0.590
Mettu_1921
Thioredoxin; KEGG- mca-MCA0057 thioredoxin; TIGRFAM- Thioredoxin; PFAM- Thioredoxin domain; Belongs to the thioredoxin family (108 aa)
       
      0.590
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)
       
      0.538
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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