STRINGSTRING
STRING protein interaction network
Nodes:
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:
a 3D structure is known or predicted
Edges:
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
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
yraAGeneral stress protein; Functions in the protection against aldehyde-stress, possibly by degrading damaged proteins. (169 aa)    
Predicted Functional Partners:
yvgN
Glyoxal/methylglyoxal reductase; Reduces glyoxal and methylglyoxal (2-oxopropanal). Is not involved in the vitamin B6 biosynthesis; Belongs to the aldo/keto reductase family.
  
  
 0.779
yqiG
Putative NADH-dependent flavin oxidoreductase; 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 NADH:flavin oxidoreductase/NADH oxidase family.
  
  
 0.731
nfrAA
FMN-containing NADPH-linked nitro/flavin reductase; Reduces FMNH(2) to FMN, with NADPH as reductant. It also reduces nitroaromatic compounds, quinones and azo dyes.
  
  
 0.713
ypbG
Putative phosphoesterase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme.
  
  
 0.699
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.
  
  
 0.696
yurT
Putative methylglyoxalase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the glyoxalase I family.
  
  
 0.692
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.
  
  
 0.669
adhA
Putative dehydrogenase; Functions in the protection against aldehyde-stress. Belongs to the zinc-containing alcohol dehydrogenase family.
  
 
 0.652
yraB
Putative transcriptional regulator (MerR family); Transcriptional regulator involved in the response to aldehyde stress. Binds to the promoter region of the adhA-yraA operon, the yraC and its own promoter region; binding is unchanged in the presence of aldehydes.
  
  
 0.647
cypB
Cytochrome P450 CYP102A3; Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of a range of medium to long-chain fatty acids, with a preference for long-chain unsaturated and branched-chain fatty acids over saturated fatty acids. Hydroxylation of myristic acid occurs mainly at the omega-2 and omega-3 positions, in approximately equal proportions. Also displays a NADPH-dependent reductase activity in the C-terminal domain, which allows electron transfer from NADPH to the heme iron of the cytochrome P450 N-terminal domain.
   
 
 0.616
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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