grpE protein (Lactobacillus siliginis) - STRING interaction network

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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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Your Current Organism:

Lactobacillus siliginis

NCBI taxonomy Id: 348151
Other names: DSM 22696, JCM 16155, KCTC 3985, L. siliginis, Lactobacillus siliginis Aslam et al. 2006, NBRC 101315, strain M1-212

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
KRN95307.1	dnaJ	IV55_GL000294	IV55_GL002001	ATP-binding protein; Belongs to the ClpA/ClpB family.	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, DnaK and [...]	0.850
KRN95307.1	dnaK	IV55_GL000294	IV55_GL002002	ATP-binding protein; Belongs to the ClpA/ClpB family.	Chaperone protein dnak (heat shock protein 70) (heat shock 70 kda protein) (hsp70); Acts as a chaperone; Belongs to the heat shock protein 70 family.	0.948
KRN95307.1	groL	IV55_GL000294	IV55_GL001104	ATP-binding protein; Belongs to the ClpA/ClpB family.	Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	0.610
KRN95307.1	groS	IV55_GL000294	IV55_GL001103	ATP-binding protein; Belongs to the ClpA/ClpB family.	Chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.	0.620
KRN95307.1	grpE	IV55_GL000294	IV55_GL002003	ATP-binding protein; Belongs to the ClpA/ClpB family.	Molecular chaperone GrpE (heat shock protein); 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. [...]	0.767
KRN95307.1	hrcA	IV55_GL000294	IV55_GL002004	ATP-binding protein; Belongs to the ClpA/ClpB family.	Heat-inducible transcription repressor; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons.	0.478
KRN95307.1	hslO	IV55_GL000294	IV55_GL000967	ATP-binding protein; Belongs to the ClpA/ClpB family.	Heat shock protein Hsp33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.	0.400
clpC	dnaJ	IV55_GL001825	IV55_GL002001	Chaperone protein clpb; Belongs to the ClpA/ClpB family.	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, DnaK and [...]	0.850
clpC	dnaK	IV55_GL001825	IV55_GL002002	Chaperone protein clpb; Belongs to the ClpA/ClpB family.	Chaperone protein dnak (heat shock protein 70) (heat shock 70 kda protein) (hsp70); Acts as a chaperone; Belongs to the heat shock protein 70 family.	0.948
clpC	groL	IV55_GL001825	IV55_GL001104	Chaperone protein clpb; Belongs to the ClpA/ClpB family.	Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	0.610
clpC	groS	IV55_GL001825	IV55_GL001103	Chaperone protein clpb; Belongs to the ClpA/ClpB family.	Chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.	0.619
clpC	grpE	IV55_GL001825	IV55_GL002003	Chaperone protein clpb; Belongs to the ClpA/ClpB family.	Molecular chaperone GrpE (heat shock protein); 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. [...]	0.767
clpC	hrcA	IV55_GL001825	IV55_GL002004	Chaperone protein clpb; Belongs to the ClpA/ClpB family.	Heat-inducible transcription repressor; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons.	0.458
clpC	hslO	IV55_GL001825	IV55_GL000967	Chaperone protein clpb; Belongs to the ClpA/ClpB family.	Heat shock protein Hsp33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.	0.400
dnaJ	KRN95307.1	IV55_GL002001	IV55_GL000294	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, DnaK and [...]	ATP-binding protein; Belongs to the ClpA/ClpB family.	0.850
dnaJ	clpC	IV55_GL002001	IV55_GL001825	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, DnaK and [...]	Chaperone protein clpb; Belongs to the ClpA/ClpB family.	0.850
dnaJ	dnaK	IV55_GL002001	IV55_GL002002	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, DnaK and [...]	Chaperone protein dnak (heat shock protein 70) (heat shock 70 kda protein) (hsp70); Acts as a chaperone; Belongs to the heat shock protein 70 family.	0.999
dnaJ	groL	IV55_GL002001	IV55_GL001104	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, DnaK and [...]	Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	0.959
dnaJ	groS	IV55_GL002001	IV55_GL001103	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, DnaK and [...]	Chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.	0.889
dnaJ	grpE	IV55_GL002001	IV55_GL002003	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, DnaK and [...]	Molecular chaperone GrpE (heat shock protein); 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. [...]	0.995