STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
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
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
AHE96493.1ADP-heptose--LPS heptosyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology. (314 aa)    
Predicted Functional Partners:
AHE96495.1
3-deoxy-D-manno-octulosonic acid transferase; Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP- Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A; Belongs to the glycosyltransferase group 1 family.
  
 0.955
nuoC
NADH-quinone oxidoreductase subunit C; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; In the C-terminal section; belongs to the complex I 49 kDa subunit family.
    
   0.953
nuoC-2
NADH-quinone oxidoreductase subunit C; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; In the C-terminal section; belongs to the complex I 49 kDa subunit family.
    
   0.953
AHE96492.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.796
AHE95740.1
Bifunctional protein RfaE, domain I; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.776
AHE96491.1
Glutamate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.775
AHE95464.1
Glycerol-3-phosphate cytidylyltransferase; Catalyzes the ADP transfer from ATP to D-glycero-beta-D- manno-heptose 1-phosphate, yielding ADP-D-glycero-beta-D-manno-heptose.
 
  
 0.768
AHE95856.1
Ferredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
   0.731
nuoB
NADH dehydrogenase subunit B; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
    
   0.730
AHE95726.1
NADH dehydrogenase subunit M; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
   0.634
Your Current Organism:
Thermocrinis ruber
NCBI taxonomy Id: 75906
Other names: DSM 23557, T. ruber, strain OC 1/4, strain OC 14/7/2
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