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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.
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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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[Homology]
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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)    
Predicted Functional Partners:
yjbI
Putative thiol management oxidoreductase component; Hemoglobin-like protein that exhibits a low peroxidase activity. Its very high oxygen affinity may rule out the possibility that it is involved in oxygen transport.
  
  
 0.998
spxA
Redox-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.
  
 
 0.905
clpX
Protein unfolding ATPase required for presentation of proteins to proteases; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (By similarity). Probably the major protease that degrades proteins tagged by trans-translation.
  
  
 0.889
mecA
Adaptor protein controlling oligomerization of the AAA+ protein ClpC; Enables the recognition and targeting of unfolded and aggregated proteins to the ClpC protease or to other proteins involved in proteolysis. Acts negatively in the development of competence by binding ComK and recruiting it to the ClpCP protease. When overexpressed, inhibits sporulation. Also involved in Spx degradation by ClpC.
  
  
 0.850
trxB
Thioredoxin reductase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family.
  
  
 0.825
ytpQ
Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; PubMedId: 12719520, 21949854; Belongs to the UPF0354 family.
  
  
 0.758
trxA
Thioredoxin; Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.
  
  
 0.757
mecB
Regulator of competence and sporulation; Enables the recognition and targeting of unfolded and aggregated proteins to the ClpC protease or to other proteins involved in proteolysis. Also involved in Spx degradation by ClpC (By similarity). Acts negatively in the development of competence by binding ComK and recruiting it to the ClpCP protease. When overexpressed, inhibits sporulation.
   
  
 0.755
ysoA
Putative hydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme.
  
     0.740
rppG
Nucleoside and RNA triphosphate phosphohydrolase; Involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine, 8-oxo- dGTP) from DNA and the nucleotide pool. 8-oxo-dGTP is inserted opposite dA and dC residues of template DNA with almost equal efficiency thus leading to A.T to G.C transversions (By similarity). Functions, in conjunction with MutT, to protect vegetatively growing cells from DNA- damaging agents such as H(2)O(2) or t-BHP (t-butylhydroperoxide). The 2 proteins do not however protect spores. According to phosphohydrola [...]
  
     0.737
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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