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
Your Input:
Neighborhood
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Co-occurrence
Co-expression
Experiments
Databases
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[Homology]
Score
sdpIIntegral membrane regulator of autophagy; Immunity protein that provides protection for the cell against the toxic effects of SDP, its own SdpC-derived killing factor, and that functions as a receptor/signal transduction protein as well. Once SDP accumulates in the extracellular milieu, SdpI binds to SDP, causing sequestration of SdpR at the bacterial membrane. (207 aa)    
Predicted Functional Partners:
sdpR
Transcriptional regulator (ArsR family); Represses the transcription of the sdpIR operon and of several other operons that probably contribute to delaying commitment to sporulation.
 
  
 0.999
yfhL
SdpC immunity factor; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type f: factor.
   
  
 0.790
spbC
Killing factor SdpC; Produces a 42-residue extracellular sporulation delaying protein (SDP) that collapses the proton motive force (probably both the membrane potential and pH gradient) across the cell membrane, which leads to autolysis; may form a proton channel. Induces the lysis of other B.subtilis cells that have not entered the sporulation pathway, inducing cannibalism to provide a source of nutrients to support sporulation, and at the same time delaying commitment to the energetically expensive and irreversible onset of sporulation. Addition of SDP to liquid cultures halts growth [...]
  
  
 0.789
yizB
Putative DNA/RNA binding protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pf: putative factor.
 
  
 0.760
ydbS
Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function.
      
 0.744
sdpA
Export of killing factor; Required for the maturation of SdpC to SDP. Not required for SdpC signal peptide cleavage, secretion from the cell or disulfide bond formation.
  
  
 0.647
skfA
Sporulation killing factor A; Produces a 26-residue extracellular sporulation filling factor (SKF) that induces the lysis of other B.subtilis cells that have not entered the sporulation pathway, providing a source of nutrients to support sporulation, and at the same time delaying commitment to the energetically expensive and irreversible onset of sporulation. Can also inhibit growth of other bacteria at high concentrations. Addition of SKF to solid cultures induces killing, but it is much less effective than SDP (AC O34344). Has a role in protecting the secreted lipase LipA against pro [...]
   
  
 0.638
yitR
Hypothetical protein; Evidence 5: No homology to any previously reported sequences.
      
 0.567
fosB
Metallothiol transferase; Metallothiol transferase which confers resistance to fosfomycin by catalyzing the addition of a thiol cofactor to fosfomycin. L-cysteine is probably the physiological thiol donor.
      
 0.520
ylbP
Putative acetyltransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme.
      
 0.519
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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