sspJ protein (Bacillus subtilis) - 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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Score

sspJ

Small, acid-soluble spore protein J; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type cp: cell process (46 aa)

Predicted Functional Partners:

sspO

0.784

sspL

0.784

sspG

0.713

yurS

0.642

sspD

0.588

sspH

0.585

sspN

0.583

sspK

0.582

sspM

0.582

sspP

0.581

Your Current Organism:

Bacillus subtilis

NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
sspD	sspG	BSU13470	BSU32640	Small acid-soluble spore protein d (minor alpha/beta-type sasp); SASP are bound to spore DNA. They are double-stranded DNA- binding proteins that cause DNA to change to an a-like conformation. They protect the DNA backbone from chemical and enzymatic cleavage and are thus involved in dormant spore's high resistance to UV light	Small, acid-soluble spore protein G; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type f: factor	0.446
sspD	sspH	BSU13470	BSU08110	Small acid-soluble spore protein d (minor alpha/beta-type sasp); SASP are bound to spore DNA. They are double-stranded DNA- binding proteins that cause DNA to change to an a-like conformation. They protect the DNA backbone from chemical and enzymatic cleavage and are thus involved in dormant spore's high resistance to UV light	Small acid-soluble spore protein h (minor); Belongs to the SspH family	0.525
sspD	sspJ	BSU13470	BSU33340	Small acid-soluble spore protein d (minor alpha/beta-type sasp); SASP are bound to spore DNA. They are double-stranded DNA- binding proteins that cause DNA to change to an a-like conformation. They protect the DNA backbone from chemical and enzymatic cleavage and are thus involved in dormant spore's high resistance to UV light	Small, acid-soluble spore protein J; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type cp: cell process	0.588
sspD	sspO	BSU13470	BSU17990	Small acid-soluble spore protein d (minor alpha/beta-type sasp); SASP are bound to spore DNA. They are double-stranded DNA- binding proteins that cause DNA to change to an a-like conformation. They protect the DNA backbone from chemical and enzymatic cleavage and are thus involved in dormant spore's high resistance to UV light	Small acid-soluble spore protein o (minor); Belongs to the SspO family	0.583
sspD	sspP	BSU13470	BSU17980	Small acid-soluble spore protein d (minor alpha/beta-type sasp); SASP are bound to spore DNA. They are double-stranded DNA- binding proteins that cause DNA to change to an a-like conformation. They protect the DNA backbone from chemical and enzymatic cleavage and are thus involved in dormant spore's high resistance to UV light	Small acid-soluble spore protein p (minor); Belongs to the SspP family	0.440
sspD	yurS	BSU13470	BSU32650	Small acid-soluble spore protein d (minor alpha/beta-type sasp); SASP are bound to spore DNA. They are double-stranded DNA- binding proteins that cause DNA to change to an a-like conformation. They protect the DNA backbone from chemical and enzymatic cleavage and are thus involved in dormant spore's high resistance to UV light	Uncharacterized protein YurS; Evidence 5: No homology to any previously reported sequences; PubMedId: 9852018	0.583
sspG	sspD	BSU32640	BSU13470	Small, acid-soluble spore protein G; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type f: factor	Small acid-soluble spore protein d (minor alpha/beta-type sasp); SASP are bound to spore DNA. They are double-stranded DNA- binding proteins that cause DNA to change to an a-like conformation. They protect the DNA backbone from chemical and enzymatic cleavage and are thus involved in dormant spore's high resistance to UV light	0.446
sspG	sspH	BSU32640	BSU08110	Small, acid-soluble spore protein G; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type f: factor	Small acid-soluble spore protein h (minor); Belongs to the SspH family	0.712
sspG	sspJ	BSU32640	BSU33340	Small, acid-soluble spore protein G; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type f: factor	Small, acid-soluble spore protein J; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type cp: cell process	0.713
sspG	sspK	BSU32640	BSU08550	Small, acid-soluble spore protein G; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type f: factor	Small acid-soluble spore protein k (minor); Belongs to the SspK family	0.480
sspG	sspL	BSU32640	BSU22000	Small, acid-soluble spore protein G; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type f: factor	Small, acid-soluble spore protein L; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type cp: cell process	0.448
sspG	sspM	BSU32640	BSU22290	Small, acid-soluble spore protein G; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type f: factor	Small, acid-soluble spore protein M; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type cp: cell process	0.480
sspG	sspN	BSU32640	BSU18020	Small, acid-soluble spore protein G; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type f: factor	Small acid-soluble spore protein n (minor); Belongs to the SspN family	0.487
sspG	sspO	BSU32640	BSU17990	Small, acid-soluble spore protein G; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type f: factor	Small acid-soluble spore protein o (minor); Belongs to the SspO family	0.721
sspG	sspP	BSU32640	BSU17980	Small, acid-soluble spore protein G; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type f: factor	Small acid-soluble spore protein p (minor); Belongs to the SspP family	0.467
sspG	yurS	BSU32640	BSU32650	Small, acid-soluble spore protein G; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type f: factor	Uncharacterized protein YurS; Evidence 5: No homology to any previously reported sequences; PubMedId: 9852018	0.982
sspH	sspD	BSU08110	BSU13470	Small acid-soluble spore protein h (minor); Belongs to the SspH family	Small acid-soluble spore protein d (minor alpha/beta-type sasp); SASP are bound to spore DNA. They are double-stranded DNA- binding proteins that cause DNA to change to an a-like conformation. They protect the DNA backbone from chemical and enzymatic cleavage and are thus involved in dormant spore's high resistance to UV light	0.525
sspH	sspG	BSU08110	BSU32640	Small acid-soluble spore protein h (minor); Belongs to the SspH family	Small, acid-soluble spore protein G; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type f: factor	0.712
sspH	sspJ	BSU08110	BSU33340	Small acid-soluble spore protein h (minor); Belongs to the SspH family	Small, acid-soluble spore protein J; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type cp: cell process	0.585
sspH	sspK	BSU08110	BSU08550	Small acid-soluble spore protein h (minor); Belongs to the SspH family	Small acid-soluble spore protein k (minor); Belongs to the SspK family	0.506

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