RF_0598 protein (Rickettsia felis) - STRING interaction network

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Score

RF_0598

Unknown. (526 aa)

Predicted Functional Partners:

coxB

0.991

coxC

0.991

petB

0.970

cycM

0.956

nuoM

0.955

petA

0.949

nuoH

0.949

fbcH

0.907

nuoN1

0.870

nuoD

0.864

Your Current Organism:

Rickettsia felis

NCBI taxonomy Id: 315456
Other names: R. felis URRWXCal2, Rickettsia felis URRWXCal2, Rickettsia felis str. URRWXCal2, Rickettsia felis strain URRWXCal2

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
RF_0598	coxB	RF_0598	RF_0629	Unknown.	Cytochrome c oxidase polypeptide 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) (By similarity).	0.991
RF_0598	coxC	RF_0598	RF_1076	Unknown.	Cytochrome c oxidase subunit III.	0.991
RF_0598	cycM	RF_0598	RF_1030	Unknown.	Cytochrome c; May be involved in electron transfer from bc1 complex to aa3.	0.956
RF_0598	fbcH	RF_0598	RF_1007	Unknown.	Cytochrome c1, heme protein precursor.	0.907
RF_0598	nuoD	RF_0598	RF_0564	Unknown.	NADH dehydrogenase I chain 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.	0.864
RF_0598	nuoH	RF_0598	RF_1261	Unknown.	NADH 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.	0.949
RF_0598	nuoM	RF_0598	RF_1258	Unknown.	NADH dehydrogenase I chain M; 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).	0.955
RF_0598	nuoN1	RF_0598	RF_0854	Unknown.	NADH:ubiquinone oxidoreductase subunit 2 (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.	0.870
RF_0598	petA	RF_0598	RF_1010	Unknown.	Ubiquinol-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; Belongs to the Rieske iron-sulfur protein family.	0.949
RF_0598	petB	RF_0598	RF_1009	Unknown.	Cytochrome b; 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.	0.970
coxB	RF_0598	RF_0629	RF_0598	Cytochrome c oxidase polypeptide 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) (By similarity).	Unknown.	0.991
coxB	coxC	RF_0629	RF_1076	Cytochrome c oxidase polypeptide 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) (By similarity).	Cytochrome c oxidase subunit III.	0.999
coxB	cycM	RF_0629	RF_1030	Cytochrome c oxidase polypeptide 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) (By similarity).	Cytochrome c; May be involved in electron transfer from bc1 complex to aa3.	0.974
coxB	fbcH	RF_0629	RF_1007	Cytochrome c oxidase polypeptide 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) (By similarity).	Cytochrome c1, heme protein precursor.	0.982
coxB	nuoD	RF_0629	RF_0564	Cytochrome c oxidase polypeptide 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) (By similarity).	NADH dehydrogenase I chain 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.	0.914
coxB	nuoH	RF_0629	RF_1261	Cytochrome c oxidase polypeptide 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) (By similarity).	NADH 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.	0.998
coxB	nuoM	RF_0629	RF_1258	Cytochrome c oxidase polypeptide 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) (By similarity).	NADH dehydrogenase I chain M; 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).	0.992
coxB	nuoN1	RF_0629	RF_0854	Cytochrome c oxidase polypeptide 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) (By similarity).	NADH:ubiquinone oxidoreductase subunit 2 (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.	0.980
coxB	petA	RF_0629	RF_1010	Cytochrome c oxidase polypeptide 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) (By similarity).	Ubiquinol-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; Belongs to the Rieske iron-sulfur protein family.	0.996
coxB	petB	RF_0629	RF_1009	Cytochrome c oxidase polypeptide 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) (By similarity).	Cytochrome b; 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.	0.999