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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.