CF8_2746 protein (Nocardioides sp. CF8) - STRING interaction network

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Score

CF8_2746

Peptidase M48, Ste24p. (397 aa)

Predicted Functional Partners:

CF8_2747

0.776

CF8_2748

0.574

ftsH

0.568

secY

0.527

CF8_1222

0.425

Your Current Organism:

Nocardioides sp. CF8

NCBI taxonomy Id: 110319
Other names: N. sp. CF8

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
CF8_1222	CF8_2746	CF8_1222	CF8_2746	Hypothetical protein.	Peptidase M48, Ste24p.	0.425
CF8_2746	CF8_1222	CF8_2746	CF8_1222	Peptidase M48, Ste24p.	Hypothetical protein.	0.425
CF8_2746	CF8_2747	CF8_2746	CF8_2747	Peptidase M48, Ste24p.	Hypothetical protein.	0.776
CF8_2746	CF8_2748	CF8_2746	CF8_2748	Peptidase M48, Ste24p.	NLP/P60 protein.	0.574
CF8_2746	ftsH	CF8_2746	CF8_0310	Peptidase M48, Ste24p.	Peptidase; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family.	0.568
CF8_2746	secY	CF8_2746	CF8_0696	Peptidase M48, Ste24p.	Preprotein translocase subunit 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.	0.527
CF8_2747	CF8_2746	CF8_2747	CF8_2746	Hypothetical protein.	Peptidase M48, Ste24p.	0.776
CF8_2747	CF8_2748	CF8_2747	CF8_2748	Hypothetical protein.	NLP/P60 protein.	0.698
CF8_2748	CF8_2746	CF8_2748	CF8_2746	NLP/P60 protein.	Peptidase M48, Ste24p.	0.574
CF8_2748	CF8_2747	CF8_2748	CF8_2747	NLP/P60 protein.	Hypothetical protein.	0.698
ftsH	CF8_2746	CF8_0310	CF8_2746	Peptidase; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family.	Peptidase M48, Ste24p.	0.568
ftsH	secY	CF8_0310	CF8_0696	Peptidase; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family.	Preprotein translocase subunit 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.	0.512
secY	CF8_2746	CF8_0696	CF8_2746	Preprotein translocase subunit 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.	Peptidase M48, Ste24p.	0.527
secY	ftsH	CF8_0696	CF8_0310	Preprotein translocase subunit 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.	Peptidase; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family.	0.512