STRING protein interaction network
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
protein homology
Your Input:
Gene Fusion
spoIISATwo-component apoptosis factor (toxin/antitoxin system); Toxic component of a type II toxin-antitoxin (TA) system. Its toxic activity is neutralized by cognate antitoxin SpoIISB. Expression in the absence of SpoIISB permits sporulation to stage II, when plasmolysis zones and holes in the peptidoglycan layer are observed, resulting in cell death. Lethal when synthesized during vegetative growth in the absence of SpoIISB. In E.coli both the membrane bound and soluble domain are required in cis for toxin activity (248 aa)    
Predicted Functional Partners:
Two-component apoptotic control system component b (antitoxin); Antitoxin component of a type II toxin-antitoxin (TA) system. Antitoxin that binds cognate toxin SpoIISA and neutralizes its toxic activity; unlike most antitoxins it does not seem to be highly labile upon expression in E.coli
Copg family transcriptional regulator / antitoxin endoai; Antitoxin component of a type II toxin-antitoxin (TA) system. Antitoxin that directly inhibits activity of EndoA in vitro. Upon expression in E.coli counteracts inhibitory effect of endoribonuclease EndoA. The EndoA-EndoAI complex does not seem to bind its own promoter
Ribonuclease toxin of the rtbd-rtbe toxin-antitoxin system; Toxic component of a type II toxin-antitoxin (TA) system. The C-terminus (residues 409-569) has RNase activity, and inhibits growth upon expression in E.coli. In vitro RNase activity and in vivo growth inhibition are neutralized by cognate antitoxin YxxD, but not by antitoxins specific to other toxins with the LXG domain
Uncharacterized protein YcgB; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pm: putative membrane component
Endoribonuclease toxin; Toxic component of a type II toxin-antitoxin (TA) system. Specific for 5'-UACAU-3' sequences, cleaving after the first U . Yields cleavage products with 3' phosphate and 5' hydroxyl groups . Cannot digest substrate with a UUdUACAUAA cleavage site . Overexpression is toxic for cell growth (shown in E.coli), probably by inhibiting protein synthesis through the cleavage of single-stranded RNA. The toxicity is reversed by the antitoxin EndoAI. Toxin activity cannot be inhibited by MazE from E.coli. The EndoA-EndoAI complex does not seem to bind its own promoter
Hypothetical protein; Uncharacterized protein YitR; Evidence 5: No homology to any previously reported sequences
Dna helicase ii / atp-dependent dna helicase pcra; May be involved in the generation of recombinogenic substrates for the subsequent action of RecA
Uncharacterized protein YwrJ; Evidence 4: Homologs of previously reported genes of unknown function; PubMedId: 14762006
Degv domain-containing protein yits; May bind long-chain fatty acids, such as palmitate, and may play a role in lipid transport or fatty acid metabolism
Subunit b of dna topoisomerase iv; Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA. Performs the decatenation events required during the replication of a circular DNA molecule
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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