close STRING v12.5 is now available!
The next version of STRING is ready for use in your analyses: updated networks across STRING • newly available directed regulatory networks • a new typed view showing functional, physical, and regulatory edges in one network • new clustering options and cluster-based layouts • … and much more!
Explore STRING v12.5 →
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
AppCCytochrome D ubiquinol oxidase subunit I. (454 aa)    
Predicted Functional Partners:
CydB
Cytochrome D ubiquinol oxidase subunit II, cyanide insensitive.
 
 0.999
PutA
Bifunctional PutA protein; Oxidizes proline to glutamate for use as a carbon and nitrogen source; In the C-terminal section; belongs to the aldehyde dehydrogenase family.
   
 
 0.675
sdhA_2
Succinate dehydrogenase flavoprotein subunit; Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.
     
 0.659
sdhB
Succinate dehydrogenase iron-sulfur subunit.
     
 0.620
nuoH
NADH-quinone oxidoreductase chain 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.
     
 0.619
nuoA
NADH dehydrogenase I chain 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 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 3 family.
     
 0.602
nuoK
NADH-quinone oxidoreductase chain 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.
     
 0.599
nuoL
NADH-quinone oxidoreductase chain L.
     
 0.587
nuoN
NADH dehydrogenase I 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 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 2 family.
     
 0.587
nuoG
NADH dehydrogenase I chain G; 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.
     
 0.586
Your Current Organism:
Legionella lansingensis
NCBI taxonomy Id: 45067
Other names: ATCC 49751, CCUG 31227 B, CIP 103542, DSM 19556, L. lansingensis, NCTC 12830
Server load: medium (58%) [HD]