CAP_4463 protein (Chondromyces apiculatus) - STRING interaction network

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Score

CAP_4463

Putative lipoprotein. (440 aa)

Predicted Functional Partners:

CAP_2031

0.805

CAP_1171

0.766

CAP_2024

0.766

msrP

0.740

CAP_8575

0.740

CAP_3563

0.699

CAP_4292

0.695

CAP_7954

0.675

CAP_3724

0.669

CAP_5114

0.662

Your Current Organism:

Chondromyces apiculatus

NCBI taxonomy Id: 1192034
Other names: C. apiculatus DSM 436, Chondromyces apiculatus Cm a2, Chondromyces apiculatus DSM 436, Chondromyces apiculatus str. DSM 436, Chondromyces apiculatus strain DSM 436

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
CAP_1171	CAP_2024	CAP_1171	CAP_2024	Molybdopterin oxidoreductase, iron-sulfur binding protein subunit.	Molybdopterin oxidoreductase, iron-sulfur binding protein subunit.	0.999
CAP_1171	CAP_2031	CAP_1171	CAP_2031	Molybdopterin oxidoreductase, iron-sulfur binding protein subunit.	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).	0.999
CAP_1171	CAP_4463	CAP_1171	CAP_4463	Molybdopterin oxidoreductase, iron-sulfur binding protein subunit.	Putative lipoprotein.	0.766
CAP_1171	CAP_8575	CAP_1171	CAP_8575	Molybdopterin oxidoreductase, iron-sulfur binding protein subunit.	Sulfite oxidase.	0.791
CAP_1171	msrP	CAP_1171	CAP_7092	Molybdopterin oxidoreductase, iron-sulfur binding protein subunit.	Putative sulfite oxidase subunit YedY; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce [...]	0.791
CAP_2024	CAP_1171	CAP_2024	CAP_1171	Molybdopterin oxidoreductase, iron-sulfur binding protein subunit.	Molybdopterin oxidoreductase, iron-sulfur binding protein subunit.	0.999
CAP_2024	CAP_2031	CAP_2024	CAP_2031	Molybdopterin oxidoreductase, iron-sulfur binding protein subunit.	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).	0.999
CAP_2024	CAP_4463	CAP_2024	CAP_4463	Molybdopterin oxidoreductase, iron-sulfur binding protein subunit.	Putative lipoprotein.	0.766
CAP_2024	CAP_8575	CAP_2024	CAP_8575	Molybdopterin oxidoreductase, iron-sulfur binding protein subunit.	Sulfite oxidase.	0.791
CAP_2024	msrP	CAP_2024	CAP_7092	Molybdopterin oxidoreductase, iron-sulfur binding protein subunit.	Putative sulfite oxidase subunit YedY; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce [...]	0.791
CAP_2031	CAP_1171	CAP_2031	CAP_1171	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).	Molybdopterin oxidoreductase, iron-sulfur binding protein subunit.	0.999
CAP_2031	CAP_2024	CAP_2031	CAP_2024	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).	Molybdopterin oxidoreductase, iron-sulfur binding protein subunit.	0.999
CAP_2031	CAP_4463	CAP_2031	CAP_4463	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).	Putative lipoprotein.	0.805
CAP_2031	CAP_8575	CAP_2031	CAP_8575	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).	Sulfite oxidase.	0.822
CAP_2031	msrP	CAP_2031	CAP_7092	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).	Putative sulfite oxidase subunit YedY; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce [...]	0.822
CAP_3563	CAP_4292	CAP_3563	CAP_4292	Hypothetical protein.	Hypothetical protein.	0.739
CAP_3563	CAP_4463	CAP_3563	CAP_4463	Hypothetical protein.	Putative lipoprotein.	0.699
CAP_3563	CAP_5114	CAP_3563	CAP_5114	Hypothetical protein.	Hypothetical protein.	0.753
CAP_3724	CAP_4463	CAP_3724	CAP_4463	Hypothetical protein.	Putative lipoprotein.	0.669
CAP_3724	CAP_5114	CAP_3724	CAP_5114	Hypothetical protein.	Hypothetical protein.	0.658

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