OXB_1925 protein (Bacillus sp. OxB1) - STRING interaction network

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Score

OXB_1925

Cytochrome C oxidase subunit ctag. (311 aa)

Predicted Functional Partners:

OXB_1924

0.981

OXB_1921

0.967

OXB_1923

0.934

OXB_1922

0.895

OXB_1926

0.887

OXB_2355

0.840

OXB_1748

0.834

ctaA

0.813

OXB_2928

0.779

OXB_1928

0.773

Your Current Organism:

Bacillus sp. OxB1

NCBI taxonomy Id: 98228
Other names: B. sp. OxB-1, Bacillus sp. OxB-1

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... functional annotations:

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
OXB_1748	OXB_1921	OXB_1748	OXB_1921	Cytochrome C-553.	Heme/copper-type cytochrome/quinol oxidase; 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).	0.993
OXB_1748	OXB_1922	OXB_1748	OXB_1922	Cytochrome C-553.	Cytochrome C oxidase subunit i.	0.838
OXB_1748	OXB_1923	OXB_1748	OXB_1923	Cytochrome C-553.	Heme/copper-type cytochrome/quinol oxidase.	0.946
OXB_1748	OXB_1924	OXB_1748	OXB_1924	Cytochrome C-553.	Cytochrome C oxidase subunit 4b.	0.815
OXB_1748	OXB_1925	OXB_1748	OXB_1925	Cytochrome C-553.	Cytochrome C oxidase subunit ctag.	0.834
OXB_1748	OXB_1926	OXB_1748	OXB_1926	Cytochrome C-553.	Membrane protein.	0.453
OXB_1748	OXB_1928	OXB_1748	OXB_1928	Cytochrome C-553.	Ylba like protein.	0.753
OXB_1748	OXB_2355	OXB_1748	OXB_2355	Cytochrome C-553.	Menaquinol-cytochrome c reductase cytochrome b/c.	0.990
OXB_1748	OXB_2928	OXB_1748	OXB_2928	Cytochrome C-553.	Cytochrome C-551.	0.852
OXB_1921	OXB_1748	OXB_1921	OXB_1748	Heme/copper-type cytochrome/quinol oxidase; 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 C-553.	0.993
OXB_1921	OXB_1922	OXB_1921	OXB_1922	Heme/copper-type cytochrome/quinol oxidase; 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 C oxidase subunit i.	0.999
OXB_1921	OXB_1923	OXB_1921	OXB_1923	Heme/copper-type cytochrome/quinol oxidase; 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).	Heme/copper-type cytochrome/quinol oxidase.	0.999
OXB_1921	OXB_1924	OXB_1921	OXB_1924	Heme/copper-type cytochrome/quinol oxidase; 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 C oxidase subunit 4b.	0.999
OXB_1921	OXB_1925	OXB_1921	OXB_1925	Heme/copper-type cytochrome/quinol oxidase; 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 C oxidase subunit ctag.	0.967
OXB_1921	OXB_1926	OXB_1921	OXB_1926	Heme/copper-type cytochrome/quinol oxidase; 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).	Membrane protein.	0.706
OXB_1921	OXB_1928	OXB_1921	OXB_1928	Heme/copper-type cytochrome/quinol oxidase; 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).	Ylba like protein.	0.486
OXB_1921	OXB_2355	OXB_1921	OXB_2355	Heme/copper-type cytochrome/quinol oxidase; 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).	Menaquinol-cytochrome c reductase cytochrome b/c.	0.999
OXB_1921	OXB_2928	OXB_1921	OXB_2928	Heme/copper-type cytochrome/quinol oxidase; 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 C-551.	0.811
OXB_1921	ctaA	OXB_1921	OXB_1919	Heme/copper-type cytochrome/quinol oxidase; 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 aa3-controlling protein; 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 1 subfamily.	0.990
OXB_1922	OXB_1748	OXB_1922	OXB_1748	Cytochrome C oxidase subunit i.	Cytochrome C-553.	0.838