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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
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[Homology]
Score
yhdKNegative regulator of the activity of sigma-M; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type ph: phenotype. (96 aa)    
Predicted Functional Partners:
yhdL
Negative regulator of the activity of sigma-M; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type ph: phenotype.
  
 
 0.995
sigM
RNA polymerase ECF (extracytoplasmic function)-type sigma factor (sigma(M)); Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. Extracytoplasmic function (ECF) sigma factors are held in an inactive form by a cognate anti-sigma factor (YhdL) until released. This sigma factor is involved in the maintenance of membrane and cell wall integrity in response to environmental stresses including salt, acid, ethanol and antibiotics stress. Partially regulates transcription from a number of genes including disA.
  
  
 0.956
bcrC
Undecaprenyl pyrophosphate phosphatase; Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin; Belongs to the BcrC/YbjG family.
   
  
 0.757
ykoX
Putative integral inner membrane protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pm: putative membrane component.
   
  
 0.722
ylxW
Conserved hypothetical protein; May be involved in cell division and sporulation. Belongs to the UPF0749 family.
   
  
 0.639
ylxX
Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function.
   
  
 0.636
yacL
Putative membrane protein; An RNase; In the central section; belongs to the PINc/VapC protein family.
   
  
 0.522
yhdN
Aldo/keto reductase specific for NADPH; Aldo-keto reductase (AKR) that displays broad substrate specificity in vitro. Is able to reduce the standard AKR substrates DL- glyceraldehyde, D-erythrose, methylglyoxal, p-nitrobenzaldehyde, benzaldehyde and butyraldehyde, in the presence of NADPH. Cannot use NADH as a cosubstrate. Does not act on glucose, 2-pyridine carboxyaldehyde, fructose and xylose. The physiological function of this enzyme is not clear. May play a role in bacterial stress response and/or in detoxification of reactive aldehydes. Belongs to the aldo/keto reductase family. A [...]
       0.496
pbuE
Hypoxanthine efflux transporter; Involved in the efflux of purine ribonucleosides, such as guanosine, adenosine and inosine, as well as purine bases guanine, adenine and hypoxanthine, and purine base analogs 2,6-diaminopurine, 6- mercaptopurine and 2-fluoroadenine. Therefore plays a role in maintaining the cellular purine base pools and protecting cells against toxic purine base analogs. Modulates expression of the purR and G-box regulons.
      
 0.480
uppP
Undecaprenyl-diphosphatase; Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin; Belongs to the UppP family.
      
 0.459
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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