groL protein (Peptoniphilus harei) - 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:

Peptoniphilus harei

NCBI taxonomy Id: 54005
Other names: ATCC BAA-601, CCUG 38491, CIP 105323, DSM 10020, NCTC 13076, P. harei, Peptostreptococcus harei, Schleiferella harei

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
clpP	dnaK	HMPREF3229_01621	HMPREF3229_01264	ATP-dependent Clp endopeptidase, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family.	Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	0.720
clpP	groL	HMPREF3229_01621	HMPREF3229_01781	ATP-dependent Clp endopeptidase, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family.	Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	0.871
clpP	groS	HMPREF3229_01621	HMPREF3229_01780	ATP-dependent Clp endopeptidase, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family.	Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.	0.623
clpP	grpE	HMPREF3229_01621	HMPREF3229_01265	ATP-dependent Clp endopeptidase, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family.	Co-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-depend [...]	0.549
clpP	htpG	HMPREF3229_01621	HMPREF3229_00539	ATP-dependent Clp endopeptidase, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family.	Chaperone protein HtpG; Molecular chaperone. Has ATPase activity.	0.415
clpP	ldh	HMPREF3229_01621	HMPREF3229_00125	ATP-dependent Clp endopeptidase, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family.	KEGG: aur:HMPREF9243_0952 1.8e-60 L-lactate dehydrogenase K00016; Psort location: Cytoplasmic, score: 9.97; Belongs to the LDH/MDH superfamily.	0.768
clpP	lon1	HMPREF3229_01621	HMPREF3229_01623	ATP-dependent Clp endopeptidase, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family.	Endopeptidase La; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.	0.862
dnaK	clpP	HMPREF3229_01264	HMPREF3229_01621	Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	ATP-dependent Clp endopeptidase, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family.	0.720
dnaK	fusA_1	HMPREF3229_01264	HMPREF3229_01358	Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	Translation elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 s [...]	0.896
dnaK	groL	HMPREF3229_01264	HMPREF3229_01781	Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	0.997
dnaK	groS	HMPREF3229_01264	HMPREF3229_01780	Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.	0.981
dnaK	grpE	HMPREF3229_01264	HMPREF3229_01265	Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	Co-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-depend [...]	0.999
dnaK	htpG	HMPREF3229_01264	HMPREF3229_00539	Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	Chaperone protein HtpG; Molecular chaperone. Has ATPase activity.	0.988
dnaK	ldh	HMPREF3229_01264	HMPREF3229_00125	Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	KEGG: aur:HMPREF9243_0952 1.8e-60 L-lactate dehydrogenase K00016; Psort location: Cytoplasmic, score: 9.97; Belongs to the LDH/MDH superfamily.	0.852
dnaK	lon1	HMPREF3229_01264	HMPREF3229_01623	Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	Endopeptidase La; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.	0.925
dnaK	pyk	HMPREF3229_01264	HMPREF3229_00289	Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	Pyruvate kinase; KEGG: csc:Csac_1831 1.4e-163 pyruvate kinase; K00873 pyruvate kinase; Psort location: Cytoplasmic, score: 7.50.	0.847
dnaK	trxA	HMPREF3229_01264	HMPREF3229_01891	Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	Thioredoxin; KEGG: sis:LS215_0050 2.5e-08 thioredoxin K03671; Psort location: Cytoplasmic, score: 7.50.	0.416
fusA_1	dnaK	HMPREF3229_01358	HMPREF3229_01264	Translation elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 s [...]	Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	0.896
fusA_1	groL	HMPREF3229_01358	HMPREF3229_01781	Translation elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 s [...]	Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	0.901
fusA_1	groS	HMPREF3229_01358	HMPREF3229_01780	Translation elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 s [...]	Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.	0.681