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:
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Cooccurrence
Coexpression
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[Homology]
Score
nqrBNa+-transporting NADH:ubiquinone oxidoreductase subunit B; NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol. (410 aa)    
Predicted Functional Partners:
nqrA
Na+-transporting NADH:ubiquinone oxidoreductase subunit A; NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.
 
 
 0.994
nqrD
Na+-transporting NADH:ubiquinone oxidoreductase subunit D; NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol; Belongs to the NqrDE/RnfAE family.
 
 
 0.992
nqrC
Na+-transporting NADH:ubiquinone oxidoreductase subunit C; NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.
 
 
 0.991
nqrE
Na+-transporting NADH:ubiquinone oxidoreductase subunit E; NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol; Belongs to the NqrDE/RnfAE family.
 
 
 0.987
nqrF
Na+-transporting NADH:ubiquinone oxidoreductase subunit F; NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. The first step is catalyzed by NqrF, which accepts electrons from NADH and reduces ubiquinone-1 to ubisemiquinone by a one-electron transfer pathway.
 
 
 0.983
SEL88337.1
Thiamine biosynthesis lipoprotein; Flavin transferase that catalyzes the transfer of the FMN moiety of FAD and its covalent binding to the hydroxyl group of a threonine residue in a target flavoprotein. Belongs to the ApbE family.
 
   
 0.815
SEL88364.1
Hypothetical protein.
 
     0.601
mnmA
tRNA-specific 2-thiouridylase; Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
       0.436
rnfA
Electron transport complex protein RnfA; Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
  
   
 0.424
Your Current Organism:
Pasteurella skyensis
NCBI taxonomy Id: 97481
Other names: DSM 24204, NCIMB 13593, NCTC 13204, P. skyensis, Pasteurella skyensis Birkbeck et al. 2002, strain 95A1
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.