Fig. S1. Ceritinib concentration Multiple sequence alignments generated by

clustalw analysis of the N-termini of MtrB homologs identified in the genomes of 22 metal-reducing Shewanella strains. Fig. S2. Multiple sequence alignments generated by clustalw analysis of the N-termini of three CXXC-containing MtrB paralogs identified in the Shewanella oneidensis genome. Fig. S3. Growth of Shewanella oneidensisMR-1 wild-type (●), ∆mtrB (∆), C42A (□), and C45A (×) mutant strains with either O2 (A), DMSO (B), TMAO (C), fumarate (D), nitrite (E), thiosulfate (F), or nitrate (G) as electron acceptor. Table S1. Amino acid sequence identity (ID), similarity (Sim), expect-value (e-value), N-terminal CXXC motif (CXXC motif), number of amino acid residues

in the N-terminus (N-term length), and number of β-sheets in the C-terminus (No. β-sheets) of the MtrB homologs identified in the genomes of 22 metal-reducing Shewanella strains. Table S2. Amino acid sequence identity (ID), similarity (Sim), expect-value (e-value),108mm N-terminal CXXC motif (CXXC motif), number of amino acid residues in the N-terminus (N-term length), and number of β-sheets in the C-terminus (No. β-sheets) of the three MtrB paralogs identified in the genome of Shewanella oneidensis MR-1. Table S3. Phylogenetic affiliation (Class), amino acid sequence identity (ID, %), similarity (Sim, %), expect-value (e-value), N-terminal CXXC motif, (CXXC motif) number of amino Protein Tyrosine Kinase inhibitor acid residues in the N-terminus (N-term length), number of β-sheets in the C-terminus (No. β-sheets), and reported dissimilatory metal reduction or oxidation activity of the host strain (metal redox) for 52 MtrB homologs displaying similarity to Shewanella oneidensisMtrB. “
“Carboxy (C)-terminal processing proteases (CTP) are a relatively new group of serine proteases. Found in a broad range of organisms – bacteria, archaea, algae, plants and animals – these

proteases are involved in the C-terminal processing of proteins. In comparison with amino-terminal processing of bacterial proteins, less is known about C-terminal processing and its physiological function. Bacterial CTPs appear to Exoribonuclease influence different basal cellular processes. Although CTPs of Gram-negative bacteria are generally referred to as being localized in the periplasm, there is little experimental evidence for this. We show for the first time the subcellular localization of a CTP-3 family protein from Pseudomonas aeruginosa, named CtpA, in the periplasm by a carefully designed fractionation study. Our results provide experimental evidence for the generally accepted hypothesis that CTPs are located in the periplasmic space of Gram-negative bacteria. Carboxy (C)-terminal processing proteases (CTP) form a relatively new group of serine proteases that are involved in the C-terminal processing of proteins.