STRINGSTRING
STY0481 STY0481 STY0482 STY0482 STY0483 STY0483 STY0484 STY0484 STY0485 STY0485 STY1419 STY1419 STY2546 STY2546 STY2547 STY2547 STY2548 STY2548 nuoK nuoK STY2550 STY2550 nuoI nuoI STY2552 STY2552 nuoG nuoG STY2554 STY2554 STY2555 STY2555 STY2556 STY2556 STY2557 STY2557 STY2558 STY2558 STY2822 STY2822
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:
STY0481Cytochrome o ubiquinol oxidase C subunit; 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. (296 aa)
STY0482Cytochrome o ubiquinol oxidase C subunit; Orthologue of E. coli cyoD (CYOD_ECOLI); Fasta hit to CYOD_ECOLI (109 aa), 94% identity in 109 aa overlap. (109 aa)
STY0483Cytochrome o ubiquinol oxidase subunit III; Orthologue of E. coli cyoC (CYOC_ECOLI); Fasta hit to CYOC_ECOLI (204 aa), 97% identity in 204 aa overlap. (204 aa)
STY0484Cytochrome o ubiquinol oxidase subunit I; Orthologue of E. coli cyoB (CYOB_ECOLI); Fasta hit to CYOB_ECOLI (663 aa), 96% identity in 663 aa overlap; Belongs to the heme-copper respiratory oxidase family. (663 aa)
STY0485Cytochrome o ubiquinol oxidase subunit II; Orthologue of E. coli cyoA (CYOA_ECOLI); Fasta hit to CYOA_ECOLI (315 aa), 96% identity in 315 aa overlap. (318 aa)
STY1419Similar to Escherichia coli probable pyruvate-flavodoxin oxidoreductase ydbK SW:NIFJ_ECOLI (P52647; P77238) (1174 aa) fasta scores: E(): 0, 92.9% id in 1174 aa; Orthologue of E. coli NIFJ_ECOLI; Fasta hit to NIFJ_ECOLI (1174 aa), 93% identity in 1174 aa overlap. (1174 aa)
STY2546NADH dehydrogenase I chain 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. (425 aa)
STY2547NADH dehydrogenase I chain M; Orthologue of E. coli nuoM (NUOM_ECOLI); Fasta hit to NUOM_ECOLI (509 aa), 96% identity in 509 aa overlap. (509 aa)
STY2548NADH dehydrogenase I chain L; Fasta hit to HYFD_ECOLI (479 aa), 33% identity in 494 aa overlap; Orthologue of E. coli nuoL (NUOL_ECOLI); Fasta hit to NUOL_ECOLI (613 aa), 95% identity in 613 aa overlap. (613 aa)
nuoKNADH dehydrogenase I chain 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)
STY2550NADH dehydrogenase I chain 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. (184 aa)
nuoINADH dehydrogenase I chain 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. (180 aa)
STY2552NADH dehydrogenase I chain 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. (325 aa)
nuoGNADH dehydrogenase I chain G; 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). (910 aa)
STY2554NADH dehydrogenase I chain 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. (445 aa)
STY2555NADH dehydrogenase I chain E; 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); Belongs to the complex I 24 kDa subunit family. (166 aa)
STY2556NADH dehydrogenase I chain 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; In the N-terminal section; belongs to the complex I 30 kDa subunit family. (600 aa)
STY2557NADH dehydrogenase I chain 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. (220 aa)
STY2558NADH dehydrogenase I chain 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. (147 aa)
STY2822Putative ferredoxin; Similar to many e.g. Chromatium vinosum ferredoxin fdx SW:FER_CHRVI (P00208) (82 aa) fasta scores: E(): 3.6e-17, 60.5% id in 76 aa; Orthologue of E. coli YFHL_ECOLI; Fasta hit to YFHL_ECOLI (86 aa), 95% identity in 86 aa overlap. (86 aa)
Your Current Organism:
Salmonella enterica Typhi
NCBI taxonomy Id: 220341
Other names: S. enterica subsp. enterica serovar Typhi str. CT18, Salmonella enterica subsp. enterica serovar Typhi CT18, Salmonella enterica subsp. enterica serovar Typhi str. CT18, Salmonella enterica subsp. enterica serovar Typhi strain CT18, Salmonella typhi CT18
Server load: low (20%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.