STRINGSTRING
AEF23290.1 AEF23290.1 AEF23294.1 AEF23294.1 AEF23289.1 AEF23289.1 AEF23291.1 AEF23291.1 AEF23292.1 AEF23292.1 AEF23293.1 AEF23293.1 AEF22280.1 AEF22280.1 AEF22424.1 AEF22424.1 AEF22272.1 AEF22272.1 nuoB nuoB AEF20099.1 AEF20099.1
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
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a 3D structure is known or predicted
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Known Interactions
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experimentally determined
Predicted Interactions
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textmining
co-expression
protein homology
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[Homology]
Score
AEF23290.1PFAM: Multiple resistance and pH regulation protein F; KEGG: psa:PST_1533 multisubunit Na+/H+ antiporter, MnhF subunit. (89 aa)    
Predicted Functional Partners:
AEF23294.1
NADH dehydrogenase (quinone); KEGG: pmy:Pmen_1441 putative monovalent cation/H+ antiporter subunit A; PFAM: NADH:ubiquinone/plastoquinone oxidoreductase; NADH:ubiquinone oxidoreductase, chain 5/L, N-terminal; Na+/H+ antiporter MnhB subunit-related protein.
 
 
 0.999
AEF23289.1
Monovalent cation/proton antiporter, MnhG/PhaG subunit; KEGG: psa:PST_1534 putative monovalent cation/H+ antiporter subunit G; TIGRFAM: Na+/H+ antiporter subunit; PFAM: Na+/H+ antiporter subunit.
 
 
 0.998
AEF23291.1
PFAM: cation antiporter; KEGG: pmy:Pmen_1444 cation antiporter.
 
 
 0.998
AEF23292.1
NADH dehydrogenase (quinone); KEGG: psa:PST_1531 putative monovalent cation/H+ antiporter subunit D; PFAM: NADH:ubiquinone/plastoquinone oxidoreductase.
 
 
 0.998
AEF23293.1
PFAM: NADH-ubiquinone oxidoreductase chain 4L/K; KEGG: pmy:Pmen_1442 putative monovalent cation/H+ antiporter subunit C.
 
 
 0.998
AEF22280.1
NAD(P)H-quinone oxidoreductase subunit J; 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 C-terminal section; belongs to the complex I 49 kDa subunit family.
   
   0.884
AEF22424.1
KEGG: pmy:Pmen_2019 NADH dehydrogenase subunit L; PFAM: NADH:ubiquinone/plastoquinone oxidoreductase.
 
 
 0.793
AEF22272.1
TIGRFAM: NADH-plastoquinone oxidoreductase, chain 5; KEGG: pmy:Pmen_2422 NADH dehydrogenase subunit L; PFAM: NADH:ubiquinone/plastoquinone oxidoreductase; NADH:ubiquinone oxidoreductase, chain 5/L, N-terminal.
  
 
 0.738
nuoB
NAD(P)H-quinone oxidoreductase subunit 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.
   
   0.551
AEF20099.1
KEGG: pag:PLES_59141 putative potassium efflux transporter; TIGRFAM: K+/H+ exchanger; PFAM: Cation/H+ exchanger; Regulator of K+ conductance, N-terminal; Belongs to the monovalent cation:proton antiporter 2 (CPA2) transporter (TC 2.A.37) family.
     
 0.414
Your Current Organism:
Pseudomonas fulva
NCBI taxonomy Id: 743720
Other names: P. fulva 12-X, Pseudomonas fulva 12-X, Pseudomonas fulva str. 12-X, Pseudomonas fulva strain 12-X
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