Genes differentially expressed upon addition of GBAP to V583ΔfsrB, V583ΔfsrBΔgelE, V583ΔfsrBΔsprE and V583ΔfsrBΔgelEΔsprE strains.

Fold-change values were obtained by comparing gene expression at 10 min against 0 min post-GBAP addition, by microarray analysis.1Fold-change values were obtained by comparing gene expression at 10 min against 0 min post-GBAP addition, by microarray analysis. (+) up-regulated (−) down-regulated;2These two genes were up-regulated in the experiments done without GBAP, only in the V583ΔfsrB strain with a fold change of +7 for E3193 and +6 for EF3194;3ef0411 is part of the predicted operon ef0411-0412-0413, which encodes a mannitol specific PTS-system;4LemA-like protein likely involved in cell wall metabolism. LemA proteins contain a predicted amino terminal transmembrane helix and a short extracellular amino terminus. The exact molecular function of this protein is uncertain;5Has two predicted transmembrane helixes and a Blast search does not reveal similarity to proteins of known function. Upstream is a putative operon encoding the potassium-transporting ATPase KdpABC (EF0567–EF0569) and the two-component system KdpED (EF0570–EF0571) (TCS12) [62];6It has a predicted transmembrane domain at its N-terminus (residues 4 to 20) and the rest of the protein is located outside the cell. It has a predicted thioredoxin fold domain similar to bacteriocin accessory proteins ((http: //www.genome.jp/dbget-bin/www_bget?efa: EF0776);7Predicted to facilitate the conversion of aspartate and alpha-ketoglutarate to oxaloacetate and glutamate;8Part of the predicted operon ef1218–ef1224, which codes for a spermidine/putrescine ABC transporter;9EF1815 has 25% amino acid sequence similarity to CidR from S. aureus (http: //blast.ncbi.nlm.nih.gov/); EF1816 is a hypothetical protein with a β-lactamase domain, has no transmembrane domain, and is orthologous to PhnP, which is involved in phosphonate metabolism. EF1815 and EF1816 are located upstream of SprE (EF1817), but only EF1816 is located in the positive DNA strand.