Lche_1425 protein (Legionella cherrii) - STRING interaction network

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Score

Lche_1425

Permease. (153 aa)

Predicted Functional Partners:

Lche_1426

0.590

Lche_1427

0.590

glnD

0.492

map_2

0.492

EptA

0.403

Your Current Organism:

Legionella cherrii

NCBI taxonomy Id: 28084
Other names: ATCC 35252, CCUG 29666, CIP 103842, DSM 19213, L. cherrii, Legionella cherryi, NCTC 11976, strain ORW

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
EptA	Lche_1425	Lche_1428	Lche_1425	Sulfatase.	Permease.	0.403
EptA	Lche_1426	Lche_1428	Lche_1426	Sulfatase.	Hypothetical protein.	0.653
EptA	Lche_1427	Lche_1428	Lche_1427	Sulfatase.	Pyridine nucleotide-disulfide oxidoreductase.	0.654
Lche_1425	EptA	Lche_1425	Lche_1428	Permease.	Sulfatase.	0.403
Lche_1425	Lche_1426	Lche_1425	Lche_1426	Permease.	Hypothetical protein.	0.590
Lche_1425	Lche_1427	Lche_1425	Lche_1427	Permease.	Pyridine nucleotide-disulfide oxidoreductase.	0.590
Lche_1425	glnD	Lche_1425	Lche_1423	Permease.	PII uridylyl-transferase; 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.	0.492
Lche_1425	map_2	Lche_1425	Lche_1424	Permease.	Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.	0.492
Lche_1426	EptA	Lche_1426	Lche_1428	Hypothetical protein.	Sulfatase.	0.653
Lche_1426	Lche_1425	Lche_1426	Lche_1425	Hypothetical protein.	Permease.	0.590
Lche_1426	Lche_1427	Lche_1426	Lche_1427	Hypothetical protein.	Pyridine nucleotide-disulfide oxidoreductase.	0.838
Lche_1427	EptA	Lche_1427	Lche_1428	Pyridine nucleotide-disulfide oxidoreductase.	Sulfatase.	0.654
Lche_1427	Lche_1425	Lche_1427	Lche_1425	Pyridine nucleotide-disulfide oxidoreductase.	Permease.	0.590
Lche_1427	Lche_1426	Lche_1427	Lche_1426	Pyridine nucleotide-disulfide oxidoreductase.	Hypothetical protein.	0.838
glnD	Lche_1425	Lche_1423	Lche_1425	PII uridylyl-transferase; 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.	Permease.	0.492
glnD	map_2	Lche_1423	Lche_1424	PII uridylyl-transferase; 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.	Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.	0.849
map_2	Lche_1425	Lche_1424	Lche_1425	Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.	Permease.	0.492
map_2	glnD	Lche_1424	Lche_1423	Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.	PII uridylyl-transferase; 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.	0.849