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
rnfD_2Electron transport complex protein RnfD; Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. Belongs to the NqrB/RnfD family. (227 aa)    
Predicted Functional Partners:
rnfG
Electron transport complex protein RnfG; Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. Belongs to the RnfG family.
 
 
 0.993
rnfE
Electron transport complex protein RnfE; Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
 
 
 0.993
rnfC
Electron transport complex protein RnfC; Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfC subfamily.
 
 
 0.986
rnfD_1
Electron transport complex protein RnfD.
     0.986
rnfA
Electron transport complex protein RnfA; Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
 
 
 0.973
rnfB
Electron transport complex protein rnfB; Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfB subfamily.
 
 
 0.968
nqrE
Na(+)-translocating NADH-quinone reductase 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.
 
   
 0.805
nqrD
Na(+)-translocating NADH-quinone reductase 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.
 
   
 0.783
nth
Endonuclease III; DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'- phosphate.
  
  
 0.771
apbE
Thiamine biosynthesis lipoprotein ApbE precursor; 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.
 
  
 0.724
Your Current Organism:
Providencia rettgeri
NCBI taxonomy Id: 587
Other names: ATCC 29944, Bacterium rettgeri, CCUG 14804, CIP 103182, DSM 4542, LMG 3259, LMG:3259, NCTC 11801, P. rettgeri, Proteus rettgeri, Shigella rettgeri
Server load: medium (54%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.