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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
KML45281.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (275 aa)    
Predicted Functional Partners:
KML35994.1
Cytochrome B; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
  
 0.996
nuoH
NADH:ubiquinone oxidoreductase subunit H; 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.
   
 
 0.923
KML46457.1
NADH:ubiquinone oxidoreductase subunit M; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.923
KML35499.1
2Fe-2S ferredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.923
KML39870.1
(2Fe-2S)-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.903
KML45670.1
Menaquinol-cytochrome C reductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.902
KML35996.1
Cytochrome B oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.885
KML35734.1
Cytochrome o ubiquinol oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.885
nuoN
NADH:ubiquinone oxidoreductase subunit N; 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 a menaquinone. 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 2 family.
   
 
 0.882
nuoA
NADH:ubiquinone oxidoreductase subunit A; 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 a menaquinone. 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 3 family.
   
 
 0.862
Your Current Organism:
Bacillus firmus
NCBI taxonomy Id: 1399
Other names: ATCC 14575, B. firmus, BCRC 11730, Bacillaceae bacterium HQ2, Bacillus sp. JP44SK20, Bacillus sp. LK28, Bacillus sp. NCIM 2264, Bacillus sp. NCIM 2462, CCM 2213, CCRC 11730, CCRC:11730, CCUG 7418, CIP 52.70, DSM 12, IAM 12464, IFO 15306, JCM 2512, LMG 7125, LMG:7125, NBRC 15306, NCAIM B.01087, NCCB 48015, NCIB 9366, NCIMB 9366, NCTC 10335, NRRL B-14307, NRRL NRS-613, VKM B-498
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