STRINGSTRING
AFE07014.1 AFE07014.1 mauG mauG qcrC qcrC AFE03494.1 AFE03494.1 AFE03797.1 AFE03797.1 AFE03801.1 AFE03801.1 AFE03815.1 AFE03815.1 sdhC sdhC nuoN nuoN nqo13 nqo13 nuoL nuoL nuoK nuoK ndhG ndhG nuoF2 nuoF2 nuoE nuoE AFE03840.1 AFE03840.1 AFE03841.1 AFE03841.1 AFE04146.1 AFE04146.1 ccpA ccpA AFE04526.1 AFE04526.1 AFE04559.1 AFE04559.1 fdx fdx AFE04811.1 AFE04811.1 AFE04858.1 AFE04858.1 AFE04946.1 AFE04946.1 norV norV AFE05249.1 AFE05249.1 ydeP1 ydeP1 AFE05381.1 AFE05381.1 sdhB sdhB sdhA sdhA AFE05902.1 AFE05902.1 adhB adhB AFE06042.1 AFE06042.1 fdxA fdxA nuoA nuoA nuoB nuoB nuoC nuoC nuoD nuoD nuoF nuoF mauG1 mauG1 AFE06548.1 AFE06548.1 AFE06708.1 AFE06708.1 AFE06804.1 AFE06804.1 etfA etfA etfB etfB ywbL ywbL yedZ yedZ AFE07008.1 AFE07008.1 AFE07009.1 AFE07009.1 AFE07010.1 AFE07010.1 coxB coxB ctaD ctaD coxC coxC AFE07028.1 AFE07028.1 AFE07029.1 AFE07029.1 AFE07169.1 AFE07169.1 AFE07172.1 AFE07172.1 AFE07350.1 AFE07350.1 AFE07428.1 AFE07428.1 AFE07508.1 AFE07508.1 mauG2 mauG2 cydB cydB cydA cydA AFE07805.1 AFE07805.1 AFE07854.1 AFE07854.1 AFE07855.1 AFE07855.1 coxN coxN coxM coxM mnhD mnhD coxC1 coxC1 ctaD1 ctaD1 coxB1 coxB1 AFE07878.1 AFE07878.1 AFE07879.1 AFE07879.1 AFE07881.1 AFE07881.1 fdhA1 fdhA1 fdhA2 fdhA2
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:
AFE07014.1Putative cytochrome c oxidase subunit IV. (146 aa)
mauGDi-heme cytochrome-c peroxidase. (387 aa)
qcrCPutative lipoprotein. (240 aa)
AFE03494.1Hypothetical protein. (134 aa)
AFE03797.1Hypothetical protein. (187 aa)
AFE03801.1Putative lipoprotein. (515 aa)
AFE03815.1Cytochrome c family protein. (109 aa)
sdhCSuccinate dehydrogenase cytochrome b558 subunit. (227 aa)
nuoNNADH dehydrogenase I subunit N; 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. (520 aa)
nqo13NADH dehydrogenase I subunit M. (563 aa)
nuoLNADH dehydrogenase I subunit L. (742 aa)
nuoKNADH dehydrogenase I 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; Belongs to the complex I subunit 4L family. (100 aa)
ndhGNADH dehydrogenase I subunit J; 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. (168 aa)
nuoF2NADH dehydrogenase I subunit F; 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. (447 aa)
nuoENADH dehydrogenase I subunit E. (162 aa)
AFE03840.1Hypothetical protein. (514 aa)
AFE03841.1Hypothetical protein. (413 aa)
AFE04146.1Cation-binding protein. (162 aa)
ccpACytochrome c peroxidase. (375 aa)
AFE04526.1Hypothetical protein. (673 aa)
AFE04559.1Putative lipoprotein. (277 aa)
fdxPutative 2Fe-2S cluster assembly ferredoxin. (125 aa)
AFE04811.1Hypothetical protein. (436 aa)
AFE04858.1Hypothetical protein. (687 aa)
AFE04946.1Hypothetical protein. (92 aa)
norVMetallo-beta-lactamase family protein. (382 aa)
AFE05249.1Putative lipoprotein. (778 aa)
ydeP1Oxidoreductase alpha (molybdopterin) subunit; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (786 aa)
AFE05381.1Hypothetical protein. (479 aa)
sdhBSuccinate dehydrogenase iron-sulfur subunit. (268 aa)
sdhASuccinate dehydrogenase flavoprotein subunit. (625 aa)
AFE05902.1Cytochrome oxidase. (416 aa)
adhBPutative cytochrome c. (417 aa)
AFE06042.1Hypothetical protein. (161 aa)
fdxAFerrodoxin, 4Fe-4S; Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. (111 aa)
nuoAPutative NADH dehydrogenase I subunit A; 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. (122 aa)
nuoBNADH dehydrogenase subunit B; 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. (187 aa)
nuoCNADH dehydrogenase I subunit C; 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 30 kDa subunit family. (177 aa)
nuoDNADH dehydrogenase I subunit 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; Belongs to the complex I 49 kDa subunit family. (419 aa)
nuoFFerredoxin-related protein. (115 aa)
mauG1Di-heme cytochrome-c peroxidase. (382 aa)
AFE06548.1PE_PGRS family protein. (189 aa)
AFE06708.1Hypothetical protein. (228 aa)
AFE06804.1Hypothetical protein. (267 aa)
etfAElectron transfer flavoprotein subunit alpha. (321 aa)
etfBElectron transfer flavoprotein subunit beta. (265 aa)
ywbLFTR1 family cytochrome c family protein/iron permease. (626 aa)
yedZPutative sulfite oxidase subunit YedZ; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subuni [...] (205 aa)
AFE07008.1Putative cytochrome c. (220 aa)
AFE07009.1Hypothetical protein. (181 aa)
AFE07010.1Hypothetical protein. (186 aa)
coxBCytochrome c oxidase subunit II. (348 aa)
ctaDCytochrome c oxidase subunit I; Belongs to the heme-copper respiratory oxidase family. (558 aa)
coxCCytochrome c oxidase subunit III. (220 aa)
AFE07028.1Hypothetical protein. (433 aa)
AFE07029.1Hypothetical protein. (425 aa)
AFE07169.1Hypothetical protein. (442 aa)
AFE07172.1Putative lipoprotein. (453 aa)
AFE07350.1Rieske family iron-sulfur cluster-binding protein. (176 aa)
AFE07428.1Hypothetical protein. (293 aa)
AFE07508.1Cytochrome c family protein. (276 aa)
mauG2Cytochrome c peroxidase. (436 aa)
cydBCytochrome d ubiquinol oxidase subunit II. (343 aa)
cydACytochrome d ubiquinol oxidase subunit I. (448 aa)
AFE07805.1Hypothetical protein. (219 aa)
AFE07854.1Hypothetical protein. (332 aa)
AFE07855.1Hypothetical protein. (197 aa)
coxNAlternative cytochrome c oxidase subunit 1; Belongs to the heme-copper respiratory oxidase family. (577 aa)
coxMAlternative cytochrome c oxidase subunit 2. (278 aa)
mnhDNADH-ubiquinone/plastoquinone oxidoreductase family protein. (455 aa)
coxC1Cytochrome c oxidase subunit III. (209 aa)
ctaD1Cytochrome c oxidase subunit I; Belongs to the heme-copper respiratory oxidase family. (535 aa)
coxB1Cytochrome c oxidase subunit II. (336 aa)
AFE07878.1Hypothetical protein. (308 aa)
AFE07879.1Hypothetical protein. (176 aa)
AFE07881.1Putative cytochrome c. (216 aa)
fdhA1Formate dehydrogenase subunit alpha. (189 aa)
fdhA2Formate dehydrogenase O alpha subunit; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (892 aa)
Your Current Organism:
Corallococcus coralloides
NCBI taxonomy Id: 1144275
Other names: C. coralloides DSM 2259, Corallococcus coralloides ATCC 25202, Corallococcus coralloides DSM 2259, Corallococcus coralloides NBRC 100086, Corallococcus coralloides str. DSM 2259, Corallococcus coralloides strain DSM 2259
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