Table 2.

Proteins identified in chemical proteomic analyses

Streptomyces coelicolor	Mycobactehum smegmatis
Aconitate hydratase	Beta-lactamase
Aminolevulinic acid dehydratase	ClpB
ClpP1	ClpP1
ClpP2	ClpP2
DNA binding protein, EngD	D-alanyl-D-alanine carboxylpeptidase
Molybdenum cofactor protein, MoaC	Leucyl-tRNA synthetase
Proteasome α-subunit	Malate dehydrogenase
Pyridoxal lyase, PdxS	Purine biosynthesis protein, PurH
	Proteasome β-subunit
	Prokaryotic Ubiquitin-like Protein, PUP
	Thiosulfate sulfurtransferase
	Tryptophan synthase
	Tryptophan-tRNA synthetase

Proteins identified in both S. coelicolor and M. smegmatis are shown in bold text. In the bioinformatic identifications of the peptide fragments, a trypsin specificity with two missed cleavage sites was allowed and the MS mass tolerance was 7 ppm while the MS-MS tolerance was 0.5 Daltons. Identifications were contingent on at least one unique peptide spectrum match (psm) in the molecular weight search (MOWSE) with a protein score cut-off of 32.8. An additional information on the proteins in this list can be formed in Tables S4and S5.