htpX protein (Legionella moravica) - STRING interaction network

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[Homology]

Score

htpX

Heat shock protein HtpX; Belongs to the peptidase M48B family. (339 aa)

Predicted Functional Partners:

Lmor_2134

0.949

ftsH

0.917

dnaJ_4

0.872

yccA

0.805

grpE

0.800

secY

0.741

dnaK

0.662

hslU

0.635

yggG

0.607

Lmor_2907

0.582

Your Current Organism:

Legionella moravica

NCBI taxonomy Id: 39962
Other names: ATCC 43877, CCUG 31117, CIP 103883, DSM 19234, L. moravica, NCTC 12239, strain 316-36

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
Lmor_2134	htpX	Lmor_2134	Lmor_2133	LemA protein.	Heat shock protein HtpX; Belongs to the peptidase M48B family.	0.949
Lmor_2907	dnaJ_4	Lmor_2907	Lmor_0630	Saframycin Mx1 synthetase B.	Molecular chaperone DnaJ.	0.821
Lmor_2907	dnaK	Lmor_2907	Lmor_2614	Saframycin Mx1 synthetase B.	Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	0.692
Lmor_2907	grpE	Lmor_2907	Lmor_2615	Saframycin Mx1 synthetase B.	Heat shock protein GrpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP- [...]	0.548
Lmor_2907	htpX	Lmor_2907	Lmor_2133	Saframycin Mx1 synthetase B.	Heat shock protein HtpX; Belongs to the peptidase M48B family.	0.582
Lmor_2907	secY	Lmor_2907	Lmor_2175	Saframycin Mx1 synthetase B.	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.	0.418
dnaJ_4	Lmor_2907	Lmor_0630	Lmor_2907	Molecular chaperone DnaJ.	Saframycin Mx1 synthetase B.	0.821
dnaJ_4	dnaK	Lmor_0630	Lmor_2614	Molecular chaperone DnaJ.	Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	0.998
dnaJ_4	ftsH	Lmor_0630	Lmor_1288	Molecular chaperone DnaJ.	Cell division protease ftsH; 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.	0.843
dnaJ_4	grpE	Lmor_0630	Lmor_2615	Molecular chaperone DnaJ.	Heat shock protein GrpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP- [...]	0.958
dnaJ_4	hslU	Lmor_0630	Lmor_0834	Molecular chaperone DnaJ.	ATP-dependent protease ATP-binding subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.	0.865
dnaJ_4	htpX	Lmor_0630	Lmor_2133	Molecular chaperone DnaJ.	Heat shock protein HtpX; Belongs to the peptidase M48B family.	0.872
dnaJ_4	secY	Lmor_0630	Lmor_2175	Molecular chaperone DnaJ.	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.	0.960
dnaK	Lmor_2907	Lmor_2614	Lmor_2907	Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	Saframycin Mx1 synthetase B.	0.692
dnaK	dnaJ_4	Lmor_2614	Lmor_0630	Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	Molecular chaperone DnaJ.	0.998
dnaK	ftsH	Lmor_2614	Lmor_1288	Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	Cell division protease ftsH; 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.	0.800
dnaK	grpE	Lmor_2614	Lmor_2615	Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	Heat shock protein GrpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP- [...]	0.999
dnaK	hslU	Lmor_2614	Lmor_0834	Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	ATP-dependent protease ATP-binding subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.	0.891
dnaK	htpX	Lmor_2614	Lmor_2133	Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	Heat shock protein HtpX; Belongs to the peptidase M48B family.	0.662
dnaK	secY	Lmor_2614	Lmor_2175	Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 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.	0.866