sseJ protein (Providencia rettgeri) - STRING interaction network

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sseJ

Secreted effector protein SseJ. (370 aa)

Predicted Functional Partners:

lapB

0.542

epsF

0.541

lipA

0.533

lipB

0.533

sseL

0.486

APC09742.1

0.485

spiA

0.473

hlyD

0.466

ykgM

0.461

sseD

0.449

Your Current Organism:

Providencia rettgeri

NCBI taxonomy Id: 587
Other names: ATCC 29944, Bacterium rettgeri, CCUG 14804, CIP 103182, DSM 4542, LMG 3259, LMG:3259, NCTC 11801, P. rettgeri, Proteus rettgeri, Shigella rettgeri

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
APC09742.1	sseJ	RB151_000210	RB151_000100	Hypothetical protein.	Secreted effector protein SseJ.	0.485
epsF	spiA	RB151_030310	RB151_001170	Type II secretion system protein F.	Type III secretion system outer membrane protein SpiA precursor.	0.582
epsF	sseJ	RB151_030310	RB151_000100	Type II secretion system protein F.	Secreted effector protein SseJ.	0.541
hlyD	lapB	RB151_013090	RB151_023180	Hemolysin secretion protein D, chromosomal.	Tetratricopeptide repeat protein; Modulates cellular lipopolysaccharide (LPS) levels by regulating LpxC, which is involved in lipid A biosynthesis. May act by modulating the proteolytic activity of FtsH towards LpxC. May also coordinate assembly of proteins involved in LPS synthesis at the plasma membrane; Belongs to the LapB family.	0.503
hlyD	sseJ	RB151_013090	RB151_000100	Hemolysin secretion protein D, chromosomal.	Secreted effector protein SseJ.	0.466
lapB	hlyD	RB151_023180	RB151_013090	Tetratricopeptide repeat protein; Modulates cellular lipopolysaccharide (LPS) levels by regulating LpxC, which is involved in lipid A biosynthesis. May act by modulating the proteolytic activity of FtsH towards LpxC. May also coordinate assembly of proteins involved in LPS synthesis at the plasma membrane; Belongs to the LapB family.	Hemolysin secretion protein D, chromosomal.	0.503
lapB	lipA	RB151_023180	RB151_010510	Tetratricopeptide repeat protein; Modulates cellular lipopolysaccharide (LPS) levels by regulating LpxC, which is involved in lipid A biosynthesis. May act by modulating the proteolytic activity of FtsH towards LpxC. May also coordinate assembly of proteins involved in LPS synthesis at the plasma membrane; Belongs to the LapB family.	Lipoyl synthase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.	0.542
lapB	lipB	RB151_023180	RB151_010520	Tetratricopeptide repeat protein; Modulates cellular lipopolysaccharide (LPS) levels by regulating LpxC, which is involved in lipid A biosynthesis. May act by modulating the proteolytic activity of FtsH towards LpxC. May also coordinate assembly of proteins involved in LPS synthesis at the plasma membrane; Belongs to the LapB family.	Octanoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.	0.542
lapB	sseJ	RB151_023180	RB151_000100	Tetratricopeptide repeat protein; Modulates cellular lipopolysaccharide (LPS) levels by regulating LpxC, which is involved in lipid A biosynthesis. May act by modulating the proteolytic activity of FtsH towards LpxC. May also coordinate assembly of proteins involved in LPS synthesis at the plasma membrane; Belongs to the LapB family.	Secreted effector protein SseJ.	0.542
lipA	lapB	RB151_010510	RB151_023180	Lipoyl synthase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.	Tetratricopeptide repeat protein; Modulates cellular lipopolysaccharide (LPS) levels by regulating LpxC, which is involved in lipid A biosynthesis. May act by modulating the proteolytic activity of FtsH towards LpxC. May also coordinate assembly of proteins involved in LPS synthesis at the plasma membrane; Belongs to the LapB family.	0.542
lipA	lipB	RB151_010510	RB151_010520	Lipoyl synthase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.	Octanoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.	0.999
lipA	sseJ	RB151_010510	RB151_000100	Lipoyl synthase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.	Secreted effector protein SseJ.	0.533
lipB	lapB	RB151_010520	RB151_023180	Octanoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.	Tetratricopeptide repeat protein; Modulates cellular lipopolysaccharide (LPS) levels by regulating LpxC, which is involved in lipid A biosynthesis. May act by modulating the proteolytic activity of FtsH towards LpxC. May also coordinate assembly of proteins involved in LPS synthesis at the plasma membrane; Belongs to the LapB family.	0.542
lipB	lipA	RB151_010520	RB151_010510	Octanoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.	Lipoyl synthase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.	0.999
lipB	sseJ	RB151_010520	RB151_000100	Octanoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.	Secreted effector protein SseJ.	0.533
spiA	epsF	RB151_001170	RB151_030310	Type III secretion system outer membrane protein SpiA precursor.	Type II secretion system protein F.	0.582
spiA	sseJ	RB151_001170	RB151_000100	Type III secretion system outer membrane protein SpiA precursor.	Secreted effector protein SseJ.	0.473
sseD	sseJ	RB151_000880	RB151_000100	Secreted effector protein SseD.	Secreted effector protein SseJ.	0.449
sseJ	APC09742.1	RB151_000100	RB151_000210	Secreted effector protein SseJ.	Hypothetical protein.	0.485
sseJ	epsF	RB151_000100	RB151_030310	Secreted effector protein SseJ.	Type II secretion system protein F.	0.541

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