PSPTO098 protein (Photobacterium profundum) - STRING interaction network

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PSPTO098

Putative reductase; 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 both (R-) and (S-) [...] (340 aa)

Predicted Functional Partners:

SF2019

0.997

CV0599

0.761

PSPTO200

0.684

PETJ

0.684

PBPRB0863

0.684

SMA1276

0.684

AGR_C_42-2

0.670

SO4723

0.537

VVA0408

0.528

STM0781

0.493

Your Current Organism:

Photobacterium profundum

NCBI taxonomy Id: 298386
Other names: P. profundum SS9, Photobacterium SS9, Photobacterium profundum SS9, Photobacterium profundum str. SS9, Photobacterium profundum strain SS9, Photobacterium sp. (strain SS9), Photobacterium sp. SS9, deep-sea eubacterium SS9

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
AGR_C_42-2	PSPTO098	PBPRA2264	PBPRB0739	Putative transthyretin family protein; Predicted by orpheus program; predicted by glimmer program; Belongs to the transthyretin family. 5-hydroxyisourate hydrolase subfamily.	Putative reductase; 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 both (R-) and (S-) [...]	0.670
AGR_C_42-2	SF2019	PBPRA2264	PBPRB0738	Putative transthyretin family protein; Predicted by orpheus program; predicted by glimmer program; Belongs to the transthyretin family. 5-hydroxyisourate hydrolase subfamily.	Hypothetical inner membrane protein; 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. MsrQ provides electrons for reduction to the reductase catalytic subunit [...]	0.835
CV0599	PBPRB0863	PBPRA0167	PBPRB0863	Putative 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).	Hypothetical protein; Predicted by orpheus program; predicted by glimmer program.	0.777
CV0599	PETJ	PBPRA0167	PBPRB0651	Putative 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).	Hypothetical protein; Predicted by orpheus program; predicted by glimmer program.	0.747
CV0599	PSPTO098	PBPRA0167	PBPRB0739	Putative 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 reductase; 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 both (R-) and (S-) [...]	0.761
CV0599	PSPTO200	PBPRA0167	PBPRA1834	Putative 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 oxidase, subunit CcoP; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex.	0.762
CV0599	SMA1276	PBPRA0167	PBPRB1053	Putative 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 nitric-oxide reductase; Predicted by orpheus program; predicted by glimmer program.	0.747
CV0599	VVA0408	PBPRA0167	PBPRB0302	Putative 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).	Conserved hypothetical protein; Predicted by orpheus program; predicted by glimmer program.	0.473
PBPRB0863	CV0599	PBPRB0863	PBPRA0167	Hypothetical protein; Predicted by orpheus program; predicted by glimmer program.	Putative 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).	0.777
PBPRB0863	PSPTO098	PBPRB0863	PBPRB0739	Hypothetical protein; Predicted by orpheus program; predicted by glimmer program.	Putative reductase; 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 both (R-) and (S-) [...]	0.684
PETJ	CV0599	PBPRB0651	PBPRA0167	Hypothetical protein; Predicted by orpheus program; predicted by glimmer program.	Putative 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).	0.747
PETJ	PSPTO098	PBPRB0651	PBPRB0739	Hypothetical protein; Predicted by orpheus program; predicted by glimmer program.	Putative reductase; 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 both (R-) and (S-) [...]	0.684
PSPTO098	AGR_C_42-2	PBPRB0739	PBPRA2264	Putative reductase; 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 both (R-) and (S-) [...]	Putative transthyretin family protein; Predicted by orpheus program; predicted by glimmer program; Belongs to the transthyretin family. 5-hydroxyisourate hydrolase subfamily.	0.670
PSPTO098	CV0599	PBPRB0739	PBPRA0167	Putative reductase; 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 both (R-) and (S-) [...]	Putative 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).	0.761
PSPTO098	PBPRB0863	PBPRB0739	PBPRB0863	Putative reductase; 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 both (R-) and (S-) [...]	Hypothetical protein; Predicted by orpheus program; predicted by glimmer program.	0.684
PSPTO098	PETJ	PBPRB0739	PBPRB0651	Putative reductase; 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 both (R-) and (S-) [...]	Hypothetical protein; Predicted by orpheus program; predicted by glimmer program.	0.684
PSPTO098	PSPTO200	PBPRB0739	PBPRA1834	Putative reductase; 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 both (R-) and (S-) [...]	Putative cytochrome c oxidase, subunit CcoP; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex.	0.684
PSPTO098	SF2019	PBPRB0739	PBPRB0738	Putative reductase; 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 both (R-) and (S-) [...]	Hypothetical inner membrane protein; 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. MsrQ provides electrons for reduction to the reductase catalytic subunit [...]	0.997
PSPTO098	SMA1276	PBPRB0739	PBPRB1053	Putative reductase; 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 both (R-) and (S-) [...]	Putative nitric-oxide reductase; Predicted by orpheus program; predicted by glimmer program.	0.684
PSPTO098	SO4723	PBPRB0739	PBPRA1893	Putative reductase; 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 both (R-) and (S-) [...]	Putative molybdopterin biosynthesis MoeAprotein; Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP. Belongs to the MoeA family.	0.537

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