, 1991). In these proteins, the conserved histidine residues act to co-ordinate an oxo-bridged di-iron cluster (Fe-O-Fe) that functions as part of the reaction center (Fox et al., 1993; Shanklin et al., 1994). The closest OlsE homologs
are present in all the sequenced Agrobacterium strains, Rhodospirillum centenum, Parvibaculum lamentivorans, Verrucomicrobium spinosum, Micavibrio aeruginosavorus, Y-27632 cell line and Azospirillum amazonense. More distant homologs are present in several actinomycetes, a few Gammaproteobacteria, and a few other Alphaproteobacteria (Table S1). No growth phenotype was observed for the OlsE–deficient mutant at increased temperatures or under pH stress conditions. Bean plants infected with OlsE-deficient mutants presented less red nodules and more white
nodules than plants infected with the wild type. Nitrogen fixation of nodules from OlsE mutant-infected plants was clearly reduced (Vences-Guzmán et al., 2011). In G. cerinus, a taurine residue can be amide-linked to the α-amino group of the ornithine moiety of OL (Tahara et al., b). It has been shown that a cell-free protein crude extract from G. cerinus contains an enzymatic activity responsible for the transfer of taurine to OL hydroxylated in the 2-position of the piggy-back fatty acid. This taurine transfer activity depends on the presence of ATP and bivalent cations (Tahara et al., b). As no G. cerinus strain has been sequenced so far, a bioinformatic search for Ibrutinib datasheet candidate genes/proteins has not been possible. The wealth of genome sequence information that has been produced in recent years allows for an accurate analysis of the distribution of OL biosynthesis
genes. Genes coding for OlsB have a high predictive value, and it should be possible to predict the capacity of an organism to synthesize OL from the presence of the olsB gene. In many cases, where the olsB gene is phylogenetically less well conserved, the fact that olsB often occurs in an operon with olsA is of help. For the purpose of predicting the distribution of OLs, we analyzed all sequenced bacterial genomes for the presence of a gene encoding an OlsB homolog. BLAST searches with OlsB sequences from S. meliloti and B. cenocepacia pick up OlsB homologs in about 25% of the sequenced bacterial species which belong to the Alpha-, Beta-, Gamma-, Deltaproteobacteria, Actinomycetales, spirochetes, Glutamate dehydrogenase green nonsulfur bacteria, verrucomicrobia, firmicutes, Aquificales, and cyanobacteria (Table S1). Within the class Alphaproteobacteria, OlsB homologs can be detected in most sequenced species belonging to the orders Rhizobiales, Rhodobacterales, and Rhodospirillales, but are generally absent from species belonging to the orders Caulobacterales, Rickettsiales, and Sphingomonadales. OlsB can also be detected in the majority of sequenced Betaproteobacteria, including most Burkholderiales and many Neisseriales, but are absent from the Nitrosomonales.