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
AFV90119.1NmrA family protein. (179 aa)    
Predicted Functional Partners:
AFV90407.1
NADH-quinone oxidoreductase; 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. Belongs to the complex I 75 kDa subunit family.
   
 0.896
AFV90408.1
NADH oxidoreductase (Quinone), F subunit; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family.
   
 0.872
AFV89049.1
Tat (Twin-arginine translocation) pathway signal sequence.
  
 
 0.840
AFV90385.1
Complex1_30kDa multi-domain protein.
   
 0.838
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 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 30 kDa subunit family.
   
 0.838
AFV90384.1
4Fe-4S binding domain-containing protein.
   
 0.830
nuoI
NADH-quinone oxidoreductase subunit I; 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.
   
 0.830
AFV90401.1
Proton-translocating NADH-quinone oxidoreductase, chain M.
   
 0.827
nuoD
NADH-quinone oxidoreductase subunit D; 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 49 kDa subunit family.
   
 0.827
AFV90413.1
NADH-quinone oxidoreductase subunit; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain.
   
 0.827
Your Current Organism:
Acidipropionibacterium acidipropionici
NCBI taxonomy Id: 1171373
Other names: A. acidipropionici ATCC 4875, Acidipropionibacterium acidipropionici ATCC 4875, Acidipropionibacterium acidipropionici DSM 20272, Acidipropionibacterium acidipropionici JCM 6432, Propionibacterium acidipropionici ATCC 4875, Propionibacterium acidipropionici DSM 20272, Propionibacterium acidipropionici JCM 6432
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