STRINGSTRING
petA petA petB petB petC petC nuoN nuoN nuoM nuoM nuoL nuoL nuoK nuoK nuoJ nuoJ nuoI nuoI nuoH nuoH nuoG nuoG nuoF nuoF nuoE nuoE nuoCD nuoCD nuoB nuoB nuoA nuoA SO_1251 SO_1251 SO_2930 SO_2930 SO_3750 SO_3750 SO_3907 SO_3907 SO_4142 SO_4142 SO_4538 SO_4538 coxB coxB coxA coxA coxC coxC SO_4811 SO_4811
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.
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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:
petAUbiquinol-cytochrome c reductase FeS subunit PetA; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. (196 aa)
petBUbiquinol-cytochrome c reductase cytochrome b subunit PetB; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. (404 aa)
petCUbiquinol-cytochrome c reductase cytochrome c1 subunit PetC. (231 aa)
nuoNNADH-ubiquinone oxidoreductase subunit N NuoN; 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 subunit 2 family. (487 aa)
nuoMNADH-ubiquinone oxidoreductase subunit M NuoM. (514 aa)
nuoLNADH-ubiquinone oxidoreductase subunit L NuoL. (615 aa)
nuoKNADH-ubiquinone oxidoreductase subunit K NuoK; 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 subunit 4L family. (102 aa)
nuoJNADH-ubiquinone oxidoreductase subunit J NuoJ; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. 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. (183 aa)
nuoINADH-ubiquinone oxidoreductase subunit I NuoI; 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. (180 aa)
nuoHNADH-ubiquinone oxidoreductase subunit H NuoH; 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. This subunit may bind ubiquinone. (322 aa)
nuoGNADH-ubiquinone oxidoreductase subunit G NuoG; 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 (By similarity). (909 aa)
nuoFNADH-ubiquinone oxidoreductase subunit F NuoF; 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. (461 aa)
nuoENADH-ubiquinone oxidoreductase subunit E NuoE. (180 aa)
nuoCDNADH-ubiquinone oxidoreductase subunit CD NuoCD; 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. (601 aa)
nuoBNADH-ubiquinone oxidoreductase subunit B NuoB; 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. (224 aa)
nuoANADH-ubiquinone oxidoreductase subunit A NuoA; 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 subunit 3 family. (134 aa)
SO_1251Ferredoxin 4Fe-4S. (83 aa)
SO_2930Bifunctional pectinolytic enzyme/cytochrome c. (907 aa)
SO_3750Predicted non-catalytic member of peptidase subfamily M16B. (471 aa)
SO_3907Cytochrome oxidase copper metallochaperone. (160 aa)
SO_4142Periplasmic monoheme cytochrome c. (109 aa)
SO_4538Predicted non-catalytic member of peptidase subfamily M16B. (492 aa)
coxBAa3-type cytochrome c oxidase subunit II CoxB; 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). (513 aa)
coxAAa3 type cytochrome c oxidase subunit I CoxA; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. (530 aa)
coxCAa3 type cytochrome c oxidase subunit III CoxC. (291 aa)
SO_4811Periplasmic peptidase family M16B. (443 aa)
Your Current Organism:
Shewanella oneidensis
NCBI taxonomy Id: 211586
Other names: S. oneidensis MR-1, Shewanella oneidensis ATCC 700550, Shewanella oneidensis MR-1, Shewanella oneidensis str. MR-1, Shewanella oneidensis strain MR-1, Shewanella sp. MR-1
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