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
KPL74414.1Hypothetical protein; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. 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. (166 aa)    
Predicted Functional Partners:
KPL74413.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
  0.960
KPL74411.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+.
    
  0.835
KPL74409.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
  0.814
nuoH
NADH-quinone oxidoreductase; 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. This subunit may bind ubiquinone.
    
  0.658
nuoK
NADH:ubiquinone oxidoreductase subunit K; 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; Belongs to the complex I subunit 4L family.
    
  0.551
nuoK-2
NADH-ubiquinone oxidoreductase subunit 4L; 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; Belongs to the complex I subunit 4L family.
    
  0.551
KPL76671.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
  0.545
KPL76440.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
  0.544
KPL74192.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
  0.544
KPL78162.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
  0.461
Your Current Organism:
Bellilinea caldifistulae
NCBI taxonomy Id: 360411
Other names: B. caldifistulae, Bellilinea caldifistulae Yamada et al. 2007, DSM 17877, JCM 13669, anaerobic filamentous bacterium GOMI-1, strain GOMI-1
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