glnK protein (Legionella erythra) - STRING interaction network

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Score

glnK

Carbamoylphosphate synthase large subunit; Belongs to the P(II) protein family. (113 aa)

Predicted Functional Partners:

Lery_2464

0.968

glnD

0.966

glnA

0.806

Lery_0496

0.745

comM

0.671

abcT3

0.655

nadE

0.642

Lery_0105

0.608

Lery_1581

0.606

Lery_0191

0.596

Your Current Organism:

Legionella erythra

NCBI taxonomy Id: 448
Other names: ATCC 35303, CCUG 29667, CIP 103843, DSM 17644, JCM 7564, L. erythra, NCTC 11977, strain SE-32A-C8

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
Lery_0105	Lery_2464	Lery_0105	Lery_2464	Adenylyl transferase; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transduction protein PII (GlnB [...]	Response regulator receiver domain protein.	0.589
Lery_0105	glnA	Lery_0105	Lery_1154	Adenylyl transferase; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transduction protein PII (GlnB [...]	Glutamine synthetase.	0.853
Lery_0105	glnD	Lery_0105	Lery_1033	Adenylyl transferase; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transduction protein PII (GlnB [...]	protein-PII uridylyltransferase; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen metabolism.	0.876
Lery_0105	glnK	Lery_0105	Lery_0495	Adenylyl transferase; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transduction protein PII (GlnB [...]	Carbamoylphosphate synthase large subunit; Belongs to the P(II) protein family.	0.608
Lery_0105	nadE	Lery_0105	Lery_2010	Adenylyl transferase; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transduction protein PII (GlnB [...]	Glutamine dependent NAD+ synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source.	0.536
Lery_0191	glnK	Lery_0191	Lery_0495	Hypothetical protein.	Carbamoylphosphate synthase large subunit; Belongs to the P(II) protein family.	0.596
Lery_0496	comM	Lery_0496	Lery_0497	Membrane fusogenic activity.	Competence related protein ComM.	0.753
Lery_0496	glnK	Lery_0496	Lery_0495	Membrane fusogenic activity.	Carbamoylphosphate synthase large subunit; Belongs to the P(II) protein family.	0.745
Lery_1581	glnK	Lery_1581	Lery_0495	Methyltransferase.	Carbamoylphosphate synthase large subunit; Belongs to the P(II) protein family.	0.606
Lery_2464	Lery_0105	Lery_2464	Lery_0105	Response regulator receiver domain protein.	Adenylyl transferase; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transduction protein PII (GlnB [...]	0.589
Lery_2464	glnA	Lery_2464	Lery_1154	Response regulator receiver domain protein.	Glutamine synthetase.	0.795
Lery_2464	glnD	Lery_2464	Lery_1033	Response regulator receiver domain protein.	protein-PII uridylyltransferase; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen metabolism.	0.551
Lery_2464	glnK	Lery_2464	Lery_0495	Response regulator receiver domain protein.	Carbamoylphosphate synthase large subunit; Belongs to the P(II) protein family.	0.968
Lery_2464	nadE	Lery_2464	Lery_2010	Response regulator receiver domain protein.	Glutamine dependent NAD+ synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source.	0.749
abcT3	glnK	Lery_0822	Lery_0495	ABC transporter ATP binding protein.	Carbamoylphosphate synthase large subunit; Belongs to the P(II) protein family.	0.655
comM	Lery_0496	Lery_0497	Lery_0496	Competence related protein ComM.	Membrane fusogenic activity.	0.753
comM	glnK	Lery_0497	Lery_0495	Competence related protein ComM.	Carbamoylphosphate synthase large subunit; Belongs to the P(II) protein family.	0.671
glnA	Lery_0105	Lery_1154	Lery_0105	Glutamine synthetase.	Adenylyl transferase; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transduction protein PII (GlnB [...]	0.853
glnA	Lery_2464	Lery_1154	Lery_2464	Glutamine synthetase.	Response regulator receiver domain protein.	0.795
glnA	glnD	Lery_1154	Lery_1033	Glutamine synthetase.	protein-PII uridylyltransferase; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen metabolism.	0.692