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A putative multicopper protein secreted by an atypical type II secretion system involved in the reduction of insoluble electron acceptors in Geobacter sulfurreducens, by T. Mehta, S. E. Childers, R. Glaven, D. R. Lovley and T. Mester

Microbiology vol. 152, part 8, pp. 2257 - 2264

Fig. S1. Genetic arrangement of the G. sulfurreducens novel oxp gene cluster (top) in relation to the P. putida GB-1 xcm gene cluster (bottom) involved in secretion of a manganese-oxidizing factor. Arrows with identical patterns indicate amino acid sequence homology. Black arrows indicate proteins predicted to have similar functions based upon the presence of the same conserved protein motifs. Arrows with no patterns indicate no relationship. The red arrow is G. sulfurreducens oxpG, of which the amino acid sequence shows 40% identity and 60% similarity to that of xcmT3 (also in red). [PDF] (17 kb)

Fig. S2. Expression of oxpG measured by RT-PCR. RNAs were extracted from wild-type cells grown in the presence of 30 mM Mn(IV) (lane 1), 100 mM Fe(III) oxide (lane 2), 40 mM fumarate (lane 3), and 56 mM ferric citrate (lane 4). Negative (C-) controls were performed without cDNA synthesis, and positive controls (C+) were performed by using genomic DNA as the template. [PDF] (10 kb)

Fig. S3. Fe(III) reduction of wild-type (squares), oxpG (circles in a) and ompB (circles in b) deletion mutants grown with the soluble Fe(III) citrate as the electron acceptor. The results are the means of triplicate incubations; error bars represent the standard deviation. [PDF] (16 kb)

Fig. S4. Alignment of OmpB with MofA from Leptothrix discophora. Red colour indicates the putative copper-binding domains. Numbers above show the amino acids participating in the formation of type I , II, and III copper binding. Green shows a potential iron-binding motif. The fibronectin-like segment is shown in blue. Alignment was made by ClustalW. [PDF] (17 kb)







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