ABC1664 protein (Bacillus clausii) - STRING interaction network

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Score

ABC1664

S-adenosylmethionine (SAM)-dependent methyltransferase. (254 aa)

Predicted Functional Partners:

ABC1885

0.543

ABC1662

0.526

ABC1663

0.521

dnaJ

0.512

prmA

0.487

hepA

0.459

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
ABC1662	ABC1663	ABC1662	ABC1663	Conserved hypothetical protein; Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.	2-methylthioadenine synthetase.	0.884
ABC1662	ABC1664	ABC1662	ABC1664	Conserved hypothetical protein; Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.	S-adenosylmethionine (SAM)-dependent methyltransferase.	0.526
ABC1662	dnaJ	ABC1662	ABC1660	Conserved hypothetical protein; Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.	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, [...]	0.817
ABC1662	prmA	ABC1662	ABC1661	Conserved hypothetical protein; Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.	Ribosomal protein L11 methyltransferase; Methylates ribosomal protein L11; Belongs to the methyltransferase superfamily. PrmA family.	0.933
ABC1663	ABC1662	ABC1663	ABC1662	2-methylthioadenine synthetase.	Conserved hypothetical protein; Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.	0.884
ABC1663	ABC1664	ABC1663	ABC1664	2-methylthioadenine synthetase.	S-adenosylmethionine (SAM)-dependent methyltransferase.	0.521
ABC1663	dnaJ	ABC1663	ABC1660	2-methylthioadenine synthetase.	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, [...]	0.796
ABC1663	prmA	ABC1663	ABC1661	2-methylthioadenine synthetase.	Ribosomal protein L11 methyltransferase; Methylates ribosomal protein L11; Belongs to the methyltransferase superfamily. PrmA family.	0.904
ABC1664	ABC1662	ABC1664	ABC1662	S-adenosylmethionine (SAM)-dependent methyltransferase.	Conserved hypothetical protein; Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.	0.526
ABC1664	ABC1663	ABC1664	ABC1663	S-adenosylmethionine (SAM)-dependent methyltransferase.	2-methylthioadenine synthetase.	0.521
ABC1664	ABC1885	ABC1664	ABC1885	S-adenosylmethionine (SAM)-dependent methyltransferase.	Heptaprenyl diphosphate synthase component I.	0.543
ABC1664	dnaJ	ABC1664	ABC1660	S-adenosylmethionine (SAM)-dependent methyltransferase.	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, [...]	0.512
ABC1664	hepA	ABC1664	ABC1889	S-adenosylmethionine (SAM)-dependent methyltransferase.	Heptaprenyl diphosphate synthase component II; Belongs to the FPP/GGPP synthase family.	0.459
ABC1664	prmA	ABC1664	ABC1661	S-adenosylmethionine (SAM)-dependent methyltransferase.	Ribosomal protein L11 methyltransferase; Methylates ribosomal protein L11; Belongs to the methyltransferase superfamily. PrmA family.	0.487
ABC1885	ABC1664	ABC1885	ABC1664	Heptaprenyl diphosphate synthase component I.	S-adenosylmethionine (SAM)-dependent methyltransferase.	0.543
ABC1885	hepA	ABC1885	ABC1889	Heptaprenyl diphosphate synthase component I.	Heptaprenyl diphosphate synthase component II; Belongs to the FPP/GGPP synthase family.	0.981
dnaJ	ABC1662	ABC1660	ABC1662	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, [...]	Conserved hypothetical protein; Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.	0.817
dnaJ	ABC1663	ABC1660	ABC1663	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, [...]	2-methylthioadenine synthetase.	0.796
dnaJ	ABC1664	ABC1660	ABC1664	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, [...]	S-adenosylmethionine (SAM)-dependent methyltransferase.	0.512
dnaJ	prmA	ABC1660	ABC1661	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, [...]	Ribosomal protein L11 methyltransferase; Methylates ribosomal protein L11; Belongs to the methyltransferase superfamily. PrmA family.	0.953