Lfee_2844 protein (Legionella feeleii) - STRING interaction network

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Score

Lfee_2844

Putative Cytochrome c, class I precursor. (124 aa)

Predicted Functional Partners:

cueO

0.794

coxB

0.738

nuoI

0.562

Lfee_2845

0.524

cyc4

0.415

Your Current Organism:

Legionella feeleii

NCBI taxonomy Id: 453
Other names: ATCC 35072, CCUG 16417, CIP 103877, DSM 17645, L. feeleii, NCTC 12022, strain WO-44C

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
Lfee_2844	Lfee_2845	Lfee_2844	Lfee_2845	Putative Cytochrome c, class I precursor.	Hypothetical protein.	0.524
Lfee_2844	coxB	Lfee_2844	Lfee_0287	Putative Cytochrome c, class I precursor.	Cytochrome 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).	0.738
Lfee_2844	cueO	Lfee_2844	Lfee_2812	Putative Cytochrome c, class I precursor.	Multicopper oxidase.	0.794
Lfee_2844	cyc4	Lfee_2844	Lfee_1699	Putative Cytochrome c, class I precursor.	Cytochrome c4.	0.415
Lfee_2844	nuoI	Lfee_2844	Lfee_1901	Putative Cytochrome c, class I precursor.	NADH 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.	0.562
Lfee_2845	Lfee_2844	Lfee_2845	Lfee_2844	Hypothetical protein.	Putative Cytochrome c, class I precursor.	0.524
coxB	Lfee_2844	Lfee_0287	Lfee_2844	Cytochrome 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).	Putative Cytochrome c, class I precursor.	0.738
coxB	cueO	Lfee_0287	Lfee_2812	Cytochrome 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).	Multicopper oxidase.	0.821
coxB	cyc4	Lfee_0287	Lfee_1699	Cytochrome 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).	Cytochrome c4.	0.873
coxB	nuoI	Lfee_0287	Lfee_1901	Cytochrome 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).	NADH 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.	0.923
cueO	Lfee_2844	Lfee_2812	Lfee_2844	Multicopper oxidase.	Putative Cytochrome c, class I precursor.	0.794
cueO	coxB	Lfee_2812	Lfee_0287	Multicopper oxidase.	Cytochrome 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).	0.821
cueO	cyc4	Lfee_2812	Lfee_1699	Multicopper oxidase.	Cytochrome c4.	0.509
cyc4	Lfee_2844	Lfee_1699	Lfee_2844	Cytochrome c4.	Putative Cytochrome c, class I precursor.	0.415
cyc4	coxB	Lfee_1699	Lfee_0287	Cytochrome c4.	Cytochrome 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).	0.873
cyc4	cueO	Lfee_1699	Lfee_2812	Cytochrome c4.	Multicopper oxidase.	0.509
nuoI	Lfee_2844	Lfee_1901	Lfee_2844	NADH 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.	Putative Cytochrome c, class I precursor.	0.562
nuoI	coxB	Lfee_1901	Lfee_0287	NADH 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.	Cytochrome 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).	0.923