HD_2014 protein (Haemophilus ducreyi) - STRING interaction network

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Score

HD_2014

Hypothetical protein. (47 aa)

Predicted Functional Partners:

lipB

0.709

HD_2015

0.642

lipA

0.496

dacA

0.432

Your Current Organism:

Haemophilus ducreyi

NCBI taxonomy Id: 233412
Other names: Haemophilus ducreyi 35000HP, Haemophilus ducreyi str. 35000HP, [. ducreyi 35000HP, [Haemophilus] ducreyi 35000HP

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
HD_2014	HD_2015	HD_2014	HD_2015	Hypothetical protein.	Conserved hypothetical protein; Belongs to the UPF0250 family.	0.642
HD_2014	dacA	HD_2014	HD_2016	Hypothetical protein.	Penicillin-binding protein 5; D-alanyl-D-alanine carboxypeptidase fraction A; Belongs to the peptidase S11 family.	0.432
HD_2014	lipA	HD_2014	HD_2012	Hypothetical protein.	Lipoic acid synthetase; 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.	0.496
HD_2014	lipB	HD_2014	HD_2013	Hypothetical protein.	Lipoate-protein ligase B; 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.	0.709
HD_2015	HD_2014	HD_2015	HD_2014	Conserved hypothetical protein; Belongs to the UPF0250 family.	Hypothetical protein.	0.642
HD_2015	dacA	HD_2015	HD_2016	Conserved hypothetical protein; Belongs to the UPF0250 family.	Penicillin-binding protein 5; D-alanyl-D-alanine carboxypeptidase fraction A; Belongs to the peptidase S11 family.	0.627
HD_2015	lipA	HD_2015	HD_2012	Conserved hypothetical protein; Belongs to the UPF0250 family.	Lipoic acid synthetase; 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.	0.697
HD_2015	lipB	HD_2015	HD_2013	Conserved hypothetical protein; Belongs to the UPF0250 family.	Lipoate-protein ligase B; 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.	0.838
dacA	HD_2014	HD_2016	HD_2014	Penicillin-binding protein 5; D-alanyl-D-alanine carboxypeptidase fraction A; Belongs to the peptidase S11 family.	Hypothetical protein.	0.432
dacA	HD_2015	HD_2016	HD_2015	Penicillin-binding protein 5; D-alanyl-D-alanine carboxypeptidase fraction A; Belongs to the peptidase S11 family.	Conserved hypothetical protein; Belongs to the UPF0250 family.	0.627
dacA	lipA	HD_2016	HD_2012	Penicillin-binding protein 5; D-alanyl-D-alanine carboxypeptidase fraction A; Belongs to the peptidase S11 family.	Lipoic acid synthetase; 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.	0.441
dacA	lipB	HD_2016	HD_2013	Penicillin-binding protein 5; D-alanyl-D-alanine carboxypeptidase fraction A; Belongs to the peptidase S11 family.	Lipoate-protein ligase B; 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.	0.524
lipA	HD_2014	HD_2012	HD_2014	Lipoic acid synthetase; 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.	Hypothetical protein.	0.496
lipA	HD_2015	HD_2012	HD_2015	Lipoic acid synthetase; 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.	Conserved hypothetical protein; Belongs to the UPF0250 family.	0.697
lipA	dacA	HD_2012	HD_2016	Lipoic acid synthetase; 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.	Penicillin-binding protein 5; D-alanyl-D-alanine carboxypeptidase fraction A; Belongs to the peptidase S11 family.	0.441
lipA	lipB	HD_2012	HD_2013	Lipoic acid synthetase; 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.	Lipoate-protein ligase B; 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
lipB	HD_2014	HD_2013	HD_2014	Lipoate-protein ligase B; 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.	Hypothetical protein.	0.709
lipB	HD_2015	HD_2013	HD_2015	Lipoate-protein ligase B; 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.	Conserved hypothetical protein; Belongs to the UPF0250 family.	0.838
lipB	dacA	HD_2013	HD_2016	Lipoate-protein ligase B; 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.	Penicillin-binding protein 5; D-alanyl-D-alanine carboxypeptidase fraction A; Belongs to the peptidase S11 family.	0.524
lipB	lipA	HD_2013	HD_2012	Lipoate-protein ligase B; 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.	Lipoic acid synthetase; 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