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
norCNitric oxide reductase, cytochrome c-containing subunit; Function of homologous gene experimentally demonstrated in an other organism; enzyme. (234 aa)    
Predicted Functional Partners:
norB
Nitric-oxide reductase subunit B (Nitric oxide reductase cytochrome b subunit; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the heme-copper respiratory oxidase family.
 
  
 0.996
nuoF
NADH-quinone oxidoreductase, chain F; 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.
   
 
 0.995
ctaC
Cytochrome c oxidase polypeptide II (Cytochrome aa3 subunit 2; 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).
  
 0.995
nuoG
NADH-quinone oxidoreductase chain G; Function of homologous gene experimentally demonstrated in an other organism; enzyme.
   
 
 0.984
nuoD
NADH-quinone oxidoreductase, chain 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 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 49 kDa subunit family.
   
 
 0.983
nuoE
NADH dehydrogenase I, chain E; NDH-1, chain E; NUO5); Function of homologous gene experimentally demonstrated in an other organism; enzyme.
   
 
 0.983
nuoC
NADH-quinone oxidoreductase, chain 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; Belongs to the complex I 30 kDa subunit family.
   
 
 0.981
nuoB
NADH-quinone oxidoreductase chain 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.
   
 
 0.979
aniA
Copper-containing nitrite reductase (Major outer membrane protein Pan 1); Function of homologous gene experimentally demonstrated in an other organism; enzyme.
 
 0.973
ABZ99692.1
Putative 4-coumarate--CoA ligase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme.
   
 
 0.969
Your Current Organism:
Leptospira biflexa
NCBI taxonomy Id: 456481
Other names: L. biflexa serovar Patoc strain 'Patoc 1 (Paris)', Leptospira biflexa serovar Patoc str. ATCC 23582, Leptospira biflexa serovar Patoc strain 'Patoc 1 (Paris)', Leptospira biflexa serovar Patoc strain Patoc 1
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