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ygaF ygaF spxA spxA yjbH yjbH yosR yosR yusE yusE yoaP yoaP ywbO ywbO ytpP ytpP bdbD bdbD skfH skfH ydbP ydbP ydfQ ydfQ ykuV ykuV yneN yneN yusI yusI yyaL yyaL yyaO yyaO ahpF ahpF yuzD yuzD ahpC ahpC ytxJ ytxJ tpx tpx ytnI ytnI trxA trxA mgsR mgsR ykuU ykuU stoA stoA resA resA bsaA bsaA scuA scuA bdbA bdbA
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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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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Edges represent protein-protein associations
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
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ygaFPutative bacterioferritin comigratory protein; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events; Belongs to the peroxiredoxin family. BCP/PrxQ subfamily. (157 aa)
spxARedox-sensitive regulator enzyme; Interferes with activator-stimulated transcription by interaction with the RNA polymerase alpha-CTD. May function to globally reduce transcription of genes involved in growth- and development- promoting processes and to increase transcription of genes involved in thiol homeostasis, during periods of extreme stress. Negatively affects competence and sporulation. Its degradation by the MecA/ClpXP complex is needed for competence development; Belongs to the ArsC family. Spx subfamily. (131 aa)
yjbHPutative thiol management oxidoreductase component; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (299 aa)
yosRSPbeta phage putative thiol disulfide oxidoreductase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type h: extrachromosomal origin; Belongs to the thioredoxin family. (80 aa)
yusEPutative thiol-disulfide oxidoreductase with thioredoxin domain; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (106 aa)
yoaPConserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; Belongs to the acetyltransferase family. (251 aa)
ywbOPutative sulfur oxido-reductase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (200 aa)
ytpPPutative thiol-disulfide oxidoreductase with thioredoxin domain; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (107 aa)
bdbDThiol-disulfide oxidoreductase; Required for the stabilization, possibly via formation of a disulfide bond, of the obligatory competence protein ComGC. May be required for the stability of secreted proteins with disulfide bonds. Not required for sporulation. (222 aa)
skfHSibling killing effect; Required for production of the bacteriocin SkfA. (141 aa)
ydbPPutative thioredoxin or thiol-disulfide isomerase; Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions; Belongs to the thioredoxin family. (106 aa)
ydfQPutative thioredoxin or thiol-disulfide isomerase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (112 aa)
ykuVThiol-disulfide isomerase; Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. (148 aa)
yneNPutative membrane-bound proteins with a thioredoxin-like domain; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the thioredoxin family. (170 aa)
yusIPutative oxidoreductase with thioredoxin domain; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the ArsC family. (118 aa)
yyaLConserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; To C.elegans B0495.5. (689 aa)
yyaOConserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. (79 aa)
ahpFAlkyl hydroperoxide reductase (large subunit); Transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). (509 aa)
yuzDPutative sulfur oxido-reduction management enzyme; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (108 aa)
ahpCAlkyl hydroperoxide reductase (small subunit); Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides; Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily. (187 aa)
ytxJConserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; PubMedId: 8733232. (108 aa)
tpxPutative peroxiredoxin; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. (167 aa)
ytnIPutative redoxin; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the glutaredoxin family. (93 aa)
trxAThioredoxin; Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. (104 aa)
mgsRTranscriptional regulator of stress; Regulates transcription of a subregulon within the general stress response. Exerts positive and negative effects in response to ethanol stress. (126 aa)
ykuUPutative 2-cys peroxiredoxin; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. (180 aa)
stoAThiol-disulfide isomerase; Thiol-disulfide oxidoreductase with a reductive function, involved in spore cortex synthesis. It could be involved either in breaking disulfide bonds in cortex components or in proteins that are important for cortex synthesis, or in thiol/disulfide bond interchange. Belongs to the thioredoxin family. (165 aa)
resAExtracytoplasmic thioredoxin involved in cytochrome c maturation (lipoprotein); Thiol-disulfide oxidoreductase which is required in disulfide reduction during c-type cytochrome synthesis. May accept reducing equivalents from CcdA, leading to breakage of disulfide bonds in apocytochrome c; following this reduction heme can be covalently attached. Does not play a role in sporulation. Belongs to the thioredoxin family. ResA subfamily. (179 aa)
bsaAPutative bacillithiol peroxidase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the glutathione peroxidase family. (160 aa)
scuAAssembly factor BSco of the Cu(A) site of cytochrome c oxidase; Necessary for insertion of copper into the active site of cytochrome c oxidase. May play a role in copper homeostasis or redox signaling; Belongs to the SCO1/2 family. (193 aa)
bdbABacteriophage SPbeta thiol-disulfide oxidoreductase; Unknown; dispensable for production of the lantibiotic sublancin 168 and for competence for DNA uptake; Belongs to the thioredoxin family. (137 aa)
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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