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Table 2 Differences in protein coding capacity mirror the stress response of the organism.

From: Divergence of protein-coding capacity and regulation in the Bacillus cereus sensu lato group

Genome clusters (from Figure 2) Organisms Source or location of isolation SigB clade (from Reference #19) SigB regulon constituents
Clade A BCB4264 Bloodstream of pneumonia patient A Core SigB regulon
  BMB171 Soil A regulatory proteins,
  BC Dairy product A cardiolipin biosynthesis,
  BCG9842 Stool sample from food poisoning outbreak A efflux pumps, SOS
  BCT43 insecticide N/A functions
  BcerKBAB4 Soil A  
Clade B BCAH187 Dairy product B Core SigB regulon only
  BNC7401 Food poisoning N/A  
  BCQ Deep oil reservoir B  
  BYBT020 insecticide N/A  
  BCE Cheese spoilage B  
Clade C GBAA Bovine carcass C Core SigB regulon
  BA Bovine carcass C regulatory proteins,
  BAA Human disease C S-layer protein,
  BAS Vaccine strain C GalNac biosynthesis,
  BAH9401 Human disease C spore germination protein
  BAMEG CDC isolate C  
Clade D BACl Chimpanzee carcass D Core SigB regulon
  BALH Iraq bioweapons facility D other additions
  BCA Human blood isolate D similar to SigB Clade C
  BF83776 Human prostate wound isolate N/A  
  BCAH820 Human periodontitis D  
  BT9727 Human tissue necrosis D  
  BCZK Zebra carcass D  
  1. Comparison of our clade organisms to previously published clade structure from SigB. N/A denotes genome sequences not available at time of sig B analysis. Previously we have shown that the clades listed correspond to differences in stress responses of sigma factor B across the B. cereus sensu lato group of organisms. These differences in stress response also correlate with protein coding capacity of these organisms.