STRINGSTRING
Jann_0325 Jann_0325 Jann_0326 Jann_0326 Jann_0327 Jann_0327 Jann_0736 Jann_0736 Jann_0737 Jann_0737 atpB atpB atpE atpE atpF2 atpF2 atpF1 atpF1 Jann_0804 Jann_0804 Jann_0809 Jann_0809 Jann_0810 Jann_0810 Jann_0811 Jann_0811 Jann_0866 Jann_0866 atpH atpH atpA atpA atpG atpG atpD atpD atpC atpC ppk ppk nuoA nuoA nuoB nuoB nuoC nuoC nuoD nuoD Jann_1176 Jann_1176 Jann_1179 Jann_1179 Jann_1183 Jann_1183 nuoH nuoH nuoI nuoI Jann_1190 Jann_1190 nuoK nuoK Jann_1194 Jann_1194 Jann_1195 Jann_1195 nuoN nuoN Jann_1250 Jann_1250 Jann_1259 Jann_1259 Jann_1846 Jann_1846 Jann_2353 Jann_2353 ctaA ctaA Jann_3151 Jann_3151 ctaG ctaG ctaB ctaB Jann_3155 Jann_3155 Jann_3361 Jann_3361 Jann_3768 Jann_3768 ccoP ccoP ccoQ ccoQ ccoO ccoO ccoN ccoN Jann_3966 Jann_3966 Jann_3967 Jann_3967 Jann_3968 Jann_3968 Jann_3969 Jann_3969
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:
Jann_0325Ubiquinol-cytochrome c reductase iron-sulfur subunit; 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. (191 aa)
Jann_0326Cytochrome b/b6-like protein; 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. (451 aa)
Jann_0327Cytochrome c1. (269 aa)
Jann_0736Cytochrome bd quinol oxidase subunit 1 apoprotein. (478 aa)
Jann_0737Cytochrome bd quinol oxidase subunit 2 apoprotein. (337 aa)
atpBATP synthase F0 subcomplex A subunit; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. Belongs to the ATPase A chain family. (282 aa)
atpEATP synthase F0 subcomplex C subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. (78 aa)
atpF2H+-transporting two-sector ATPase B/B' subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (By similarity). (193 aa)
atpF1ATP synthase F0 subcomplex B subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. (190 aa)
Jann_0804Succinate dehydrogenase subunit B; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (264 aa)
Jann_0809Succinate dehydrogenase subunit A; Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily. (606 aa)
Jann_0810Succinate dehydrogenase subunit D. (123 aa)
Jann_0811Succinate dehydrogenase subunit C. (127 aa)
Jann_0866Cyclic nucleotide-regulated FAD-dependent pyridine nucleotide-disulfide oxidoreductase. (546 aa)
atpHATP synthase F1 subcomplex delta subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; Belongs to the ATPase delta chain family. (186 aa)
atpAATP synthase F1 subcomplex alpha subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. Belongs to the ATPase alpha/beta chains family. (512 aa)
atpGATP synthase F1 gamma subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. (296 aa)
atpDATP synthase F1 subcomplex beta subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits; Belongs to the ATPase alpha/beta chains family. (474 aa)
atpCATP synthase F1 subcomplex epsilon subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. (132 aa)
ppkPolyphosphate kinase; Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP). Belongs to the polyphosphate kinase 1 (PPK1) family. (724 aa)
nuoANADH dehydrogenase 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. (121 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. 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). (177 aa)
nuoCNADH dehydrogenase 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. (207 aa)
nuoDNADH dehydrogenase 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. (412 aa)
Jann_1176NADH dehydrogenase subunit E. (395 aa)
Jann_1179NADH dehydrogenase 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. (431 aa)
Jann_1183NADH dehydrogenase subunit G; 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. Belongs to the complex I 75 kDa subunit family. (672 aa)
nuoHNADH dehydrogenase subunit H; 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. (346 aa)
nuoINADH dehydrogenase 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. (164 aa)
Jann_1190NADH dehydrogenase 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. (205 aa)
nuoKNADH dehydrogenase 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. (102 aa)
Jann_1194NADH dehydrogenase subunit L. (711 aa)
Jann_1195NADH dehydrogenase subunit M. (514 aa)
nuoNNADH dehydrogenase 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. (483 aa)
Jann_1250Cytochrome-c oxidase; Belongs to the heme-copper respiratory oxidase family. (628 aa)
Jann_1259NADH dehydrogenase (quinone). (519 aa)
Jann_1846Protein of unknown function DUF344. (297 aa)
Jann_2353Protein of unknown function DUF344. (294 aa)
ctaACytochrome oxidase assembly; Catalyzes the oxidation of the C8 methyl side group on heme O porphyrin ring into a formyl group; Belongs to the COX15/CtaA family. Type 2 subfamily. (379 aa)
Jann_3151Cytochrome c oxidase subunit III. (270 aa)
ctaGCytochrome c oxidase assembly protein CtaG/Cox11; Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I; Belongs to the COX11/CtaG family. (191 aa)
ctaBProtoheme IX farnesyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group; Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily. (309 aa)
Jann_3155Cytochrome c oxidase subunit II; 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). (320 aa)
Jann_3361Inorganic diphosphatase. (307 aa)
Jann_3768Fumarate reductase/succinate dehydrogenase flavoprotein-like protein. (460 aa)
ccoPCytochrome c oxidase cbb3-type subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. (292 aa)
ccoQCytochrome c oxidase cbb3-type. (69 aa)
ccoOCytochrome c oxidase cbb3-type subunit II. (240 aa)
ccoNCytochrome c oxidase cbb3-type subunit I; Belongs to the heme-copper respiratory oxidase family. (532 aa)
Jann_3966Succinate dehydrogenase subunit B. (237 aa)
Jann_3967Hypothetical protein. (113 aa)
Jann_3968Succinate dehydrogenase subunit C. (114 aa)
Jann_3969L-aspartate oxidase. (585 aa)
Your Current Organism:
Jannaschia sp. CCS1
NCBI taxonomy Id: 290400
Other names: J. sp. CCS1
Server load: low (24%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.