aprV protein (Aquifex aeolicus) - STRING interaction network

Nodes:

Network nodes represent proteins

splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.

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query proteins and first shell of interactors

white nodes:
second shell of interactors

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proteins of unknown 3D structure

filled nodes:
a 3D structure is known or predicted

Edges:

Edges represent protein-protein associations

associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.

Known Interactions

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experimentally determined

Predicted Interactions

gene neighborhood

gene fusions

gene co-occurrence

Others

textmining

co-expression

protein homology

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[Homology]

Score

aprV

Serine protease. (560 aa)

Predicted Functional Partners:

secY

0.770

aq_1952

0.564

ctrA1

0.428

dnaK

0.426

Your Current Organism:

Aquifex aeolicus

NCBI taxonomy Id: 224324
Other names: A. aeolicus VF5, Aquifex aeolicus VF5, Aquifex aeolicus str. VF5

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
aprV	aq_1952	aq_1950	aq_1952	Serine protease.	Putative protein.	0.564
aprV	ctrA1	aq_1950	aq_724	Serine protease.	Cation transporting ATPase (E1-E2 family).	0.428
aprV	dnaK	aq_1950	aq_996	Serine protease.	Hsp70 chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	0.426
aprV	secY	aq_1950	aq_079	Serine protease.	Preprotein translocase SecY; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently (By similarity).	0.770
aq_1952	aprV	aq_1952	aq_1950	Putative protein.	Serine protease.	0.564
ctrA1	aprV	aq_724	aq_1950	Cation transporting ATPase (E1-E2 family).	Serine protease.	0.428
dnaK	aprV	aq_996	aq_1950	Hsp70 chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	Serine protease.	0.426
dnaK	secY	aq_996	aq_079	Hsp70 chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	Preprotein translocase SecY; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently (By similarity).	0.454
secY	aprV	aq_079	aq_1950	Preprotein translocase SecY; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently (By similarity).	Serine protease.	0.770
secY	dnaK	aq_079	aq_996	Preprotein translocase SecY; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently (By similarity).	Hsp70 chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	0.454