htpX protein (Bacillus clausii) - STRING interaction network

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Score

htpX

Zn-dependent protease with chaperone function; Belongs to the peptidase M48B family. (291 aa)

Predicted Functional Partners:

ABC1505

0.901

dnaJ

0.649

groEL

0.618

groES

0.611

hrcA

0.602

tufA

0.465

ABC0267

0.464

ABC1506

0.463

grpE

0.460

ABC1509

0.448

Your Current Organism:

Bacillus clausii

NCBI taxonomy Id: 66692
Other names: B. clausii KSM-K16, Bacillus clausii KSM-K16, Bacillus sp. (strain KSM-K16), Bacillus sp. KSM-K16

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
ABC0267	dnaJ	ABC0267	ABC1660	Aminoglycoside nucleotidyltransferase.	Molecular chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. 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-dependent interactions between DnaJ, [...]	0.476
ABC0267	groEL	ABC0267	ABC0882	Aminoglycoside nucleotidyltransferase.	Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	0.512
ABC0267	groES	ABC0267	ABC0881	Aminoglycoside nucleotidyltransferase.	Chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.	0.512
ABC0267	hrcA	ABC0267	ABC1657	Aminoglycoside nucleotidyltransferase.	Heat-inducible transcription repressor HrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons.	0.542
ABC0267	htpX	ABC0267	ABC1504	Aminoglycoside nucleotidyltransferase.	Zn-dependent protease with chaperone function; Belongs to the peptidase M48B family.	0.464
ABC0267	tufA	ABC0267	ABC0148	Aminoglycoside nucleotidyltransferase.	Translation elongation factor Tu; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis.	0.451
ABC1505	ABC1506	ABC1505	ABC1506	Conserved hypothetical protein.	butyryl-CoA dehydrogenase.	0.485
ABC1505	ABC1509	ABC1505	ABC1509	Conserved hypothetical protein.	enoyl-CoA hydratase.	0.474
ABC1505	htpX	ABC1505	ABC1504	Conserved hypothetical protein.	Zn-dependent protease with chaperone function; Belongs to the peptidase M48B family.	0.901
ABC1506	ABC1505	ABC1506	ABC1505	butyryl-CoA dehydrogenase.	Conserved hypothetical protein.	0.485
ABC1506	ABC1509	ABC1506	ABC1509	butyryl-CoA dehydrogenase.	enoyl-CoA hydratase.	0.985
ABC1506	htpX	ABC1506	ABC1504	butyryl-CoA dehydrogenase.	Zn-dependent protease with chaperone function; Belongs to the peptidase M48B family.	0.463
ABC1509	ABC1505	ABC1509	ABC1505	enoyl-CoA hydratase.	Conserved hypothetical protein.	0.474
ABC1509	ABC1506	ABC1509	ABC1506	enoyl-CoA hydratase.	butyryl-CoA dehydrogenase.	0.985
ABC1509	htpX	ABC1509	ABC1504	enoyl-CoA hydratase.	Zn-dependent protease with chaperone function; Belongs to the peptidase M48B family.	0.448
dnaJ	ABC0267	ABC1660	ABC0267	Molecular chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. 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-dependent interactions between DnaJ, [...]	Aminoglycoside nucleotidyltransferase.	0.476
dnaJ	groEL	ABC1660	ABC0882	Molecular chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. 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-dependent interactions between DnaJ, [...]	Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	0.921
dnaJ	groES	ABC1660	ABC0881	Molecular chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. 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-dependent interactions between DnaJ, [...]	Chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.	0.831
dnaJ	grpE	ABC1660	ABC1658	Molecular chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. 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-dependent interactions between DnaJ, [...]	Molecular chaperone 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 [...]	0.986
dnaJ	hrcA	ABC1660	ABC1657	Molecular chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. 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-dependent interactions between DnaJ, [...]	Heat-inducible transcription repressor HrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons.	0.908