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
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
yhcJPutative ABC transporter (binding lipoprotein); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type lp: lipoprotein. (276 aa)    
Predicted Functional Partners:
metP
Methionine ABC transporter, permease component; Part of the ABC transporter complex MetNPQ involved in methionine import. Responsible for the translocation of the substrate across the membrane (Probable). It has also been shown to be involved in methionine sulfoxide transport; Belongs to the binding-protein-dependent transport system permease family. CysTW subfamily.
 0.998
metN
Methionine ABC transporter (ATP-binding protein); Part of the ABC transporter complex MetNPQ involved in methionine import. Responsible for energy coupling to the transport system (Probable). It has also been shown to be involved in methionine sulfoxide transport. Belongs to the ABC transporter superfamily. Methionine importer (TC 3.A.1.24) family.
 
 0.990
metQ
Methionine ABC transporter, substrate binding lipoprotein; Part of the ABC transporter complex MetNPQ involved in methionine import. Binds the methionine and transfers it to the membrane-bound permease. It has also been shown to be involved in methionine sulfoxide transport (Probable); Belongs to the NlpA lipoprotein family.
  
 
 
0.931
ypmT
Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function.
      
 0.748
ysdB
Conserved hypothetical protein; May mediate a negative feedback loop that down-regulates the expression of the sigma-W regulon following the activation of sigma-W in response to conditions of cell envelope stress. Might interact with and inhibit the activity of the protease PrsW, or could bind to the anti-sigma-W factor RsiW and thereby protect it from PrsW-mediated cleavage.
      
 0.719
samT
Bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; enzyme.
  
  
 0.642
catD
Catechol-2,3-dioxygenase membrane subunit; Essential for growth and viability in the presence of catechol and probably involved in the detoxification of catechol.
   
  
 0.625
yybN
Conserved hypothetical protein; Evidence 7: Gene remnant.
   
  
 0.557
ypoP
Putative transcriptional regulator (MarR family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator.
   
  
 0.529
cspB
Major cold-shock protein, RNA helicase co-factor, RNA co-chaperone; Binds to the pentamer sequences ATTGG and CCAAT with highest affinity in single-stranded DNA, and also to other sequences. Has greater affinity for ATTGG than CCAAT. Can act as transcriptional activator of cold shock genes by recognizing putative ATTGG-box elements present in promoter regions of genes induced under cold shock conditions.
  
  
 0.506
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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