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
mrpDPutative K(+)/H(+) antiporter subunit D; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative transporter. (559 aa)    
Predicted Functional Partners:
mrpE
Putative Multicomponent potassium-proton antiporter, subunit E; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative transporter.
 
 0.999
mrpAB
Putative K(+)/H(+) antiporter subunit A/B; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative transporter.
 
 
0.999
mrpG
Putative Multicomponent potassium-proton antiporter, subunit G; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative transporter.
 
 
 0.998
mrpF
Putative K(+)/H(+) antiporter subunit F; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative transporter.
 
 
 0.998
mrpC
Putative K(+)/H(+) antiporter subunit C; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative transporter.
 
 
 0.998
nuoL
NADH:ubiquinone oxidoreductase, membrane subunit L; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Energymetabolism : Aerobic.
 
 
 0.934
nuoC
NADH-quinone oxidoreductase subunit C/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; In the N-terminal section; belongs to the complex I 30 kDa subunit family.
  
 
 0.933
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.
  
 
 0.697
yfhL
Putative 4Fe-4S cluster-containing protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; carrier; Energymetabolism : Electron transport.
  
 
 0.666
PP_2185
Putative Formate dehydrogenase, alpha subunit; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology.
  
 
 0.665
Your Current Organism:
Pseudomonas putida KT2440
NCBI taxonomy Id: 160488
Other names: P. putida KT2440, Pseudomonas putida (strain KT2440), Pseudomonas putida str. KT2440
Server load: medium (52%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.