sspC protein (Streptococcus sanguinis SK355)

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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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query proteins and first shell of interactors

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second shell of interactors

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proteins of unknown 3D structure

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a 3D structure is known or predicted

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Knowledge-based Evidence

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textmining

Assay-based Predictions

experimentally determined

co-expression

Genomic Predictions

gene neighborhood

gene co-occurrence

gene fusions

Your Current Organism:

Streptococcus sanguinis SK355

NCBI taxonomy Id: 888816
Other names: S. sanguinis SK355

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structured XML interaction data, according to the 'PSI-MI' data standard

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a tab-delimited file describing the names, domains and descriptions of proteins in your network

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a tab-delimited file containing all known functional terms of proteins in your network

Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
EGJ36566.1	dnaJ	HMPREF9389_2135	HMPREF9389_0166	Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase 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 [...]	0.852
EGJ36566.1	dnaK	HMPREF9389_2135	HMPREF9389_0168	Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family.	Chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	0.861
EGJ36566.1	sspC	HMPREF9389_2135	HMPREF9389_0839	Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family.	Surface protein C.	0.821
EGJ36566.1	stp	HMPREF9389_2135	HMPREF9389_0012	Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family.	Serine/threonine protein phosphatase Stp1; COG: COG0631.	0.811
EGJ37477.1	sspC	HMPREF9389_1856	HMPREF9389_0839	Ceramide glucosyltransferase.	Surface protein C.	0.770
EGJ42266.1	sspC	HMPREF9389_0739	HMPREF9389_0839	Glycosyltransferase; COG: COG1215.	Surface protein C.	0.770
alaS	dnaK	HMPREF9389_1307	HMPREF9389_0168	alanine--tRNA ligase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.	Chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	0.523
alaS	sspC	HMPREF9389_1307	HMPREF9389_0839	alanine--tRNA ligase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.	Surface protein C.	0.858
dnaJ	EGJ36566.1	HMPREF9389_0166	HMPREF9389_2135	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 [...]	Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family.	0.852
dnaJ	dnaK	HMPREF9389_0166	HMPREF9389_0168	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 DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	0.999
dnaJ	rpoB	HMPREF9389_0166	HMPREF9389_0733	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 [...]	DNA-directed RNA polymerase subunit beta; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.	0.693
dnaJ	sspC	HMPREF9389_0166	HMPREF9389_0839	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 [...]	Surface protein C.	0.845
dnaJ	stp	HMPREF9389_0166	HMPREF9389_0012	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 [...]	Serine/threonine protein phosphatase Stp1; COG: COG0631.	0.822
dnaK	EGJ36566.1	HMPREF9389_0168	HMPREF9389_2135	Chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family.	0.861
dnaK	alaS	HMPREF9389_0168	HMPREF9389_1307	Chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	alanine--tRNA ligase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.	0.523
dnaK	dnaJ	HMPREF9389_0168	HMPREF9389_0166	Chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 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 [...]	0.999
dnaK	rpoA	HMPREF9389_0168	HMPREF9389_0687	Chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	DNA-directed RNA polymerase subunit alpha; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.	0.734
dnaK	rpoB	HMPREF9389_0168	HMPREF9389_0733	Chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	DNA-directed RNA polymerase subunit beta; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.	0.635
dnaK	sspC	HMPREF9389_0168	HMPREF9389_0839	Chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	Surface protein C.	0.808
dnaK	stp	HMPREF9389_0168	HMPREF9389_0012	Chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	Serine/threonine protein phosphatase Stp1; COG: COG0631.	0.764