litoralis KT71

and Shewanella sp. ANA-3. These ORF’s are related to proteins encoded by genes located BIIB057 supplier near the transfer origin of Escherichia coli F plasmid [Q9WTE4 and Q9S4W2]. Although the function of the first protein is unknown, the second shows similarity to ParB-like nucleases initially identified as a selleck critical element in the faithful partitioning of plasmid DNA during cell division in the absence of selection pressure [34, 35]. Subsequently, a number of similar proteins have been identified in prokaryotes and archea which carry out the function of segregation of genomic DNA during cell division. ParB homologs are present in almost all eubacteria chromosomes [36]. The next region on all elements contains proteins similar of the XRE [Xenobiotic Responsive Element] family of transcriptional regulators, AZD9291 in vivo a putative lipoprotein with a DNA binding domain and a protein of unknown function. The XRE family behave as lambda repressor-like proteins associated with different phages, including Staphylococcus aureus phage phi 11 [37] and the Bacillus subtilis defective prophage PBSX [[38], Fig. 1]. Two different homologues of the XRE were found in different elements one related to that found in the original Tn4371 element (R. pickettii 12J, D. acidovorans SPH-1, A. avenae

subsp. citrulli AAC00-1, C. testosteroni KF-1 and Acidovorax sp. JS42, C. litoralis KT71, Shewanella sp. ANA-3, P. aeruginosa 2192 and P. aeruginosa PA7, P. aeruginosa PACS171b, Thioalkalivibrio sp. HL-EbGR7 and B. pseudomallei MSHR346). A different XRE was found in the remaining elements: B. petrii DSM 12804, S. maltophilia K279a, P. aeruginosa CYTH4 UCBPP-PA14, Diaphorobacter sp. TPSY, P. naphthalenivorans CJ2 plasmid pPNAP01 and the second element of Delftia acidovorans SPH-1. Following on from the XRE transcriptional regulators, a protein [ORF00035 of Tn4371] was found with similarity to the

RdfS excisionase [CAD31514] of ICEMlSymR7A, the symbiosis island of Mesorhizobium loti R7A [39]. Most excisionases, also called recombination directionality factors [RDF's], share a number of conserved features: they are small [usually <100 amino acids] DNA-binding proteins, that are typically basic with the majority of known RDFs having isoelectric points in the range of pH 8-10 [40]. The size of the ORF00035 protein homologues found in this comparative analysis ranged from 89-98 aa [amino acid] and had pI’s ranging from 8.14 to 9.59. BlastP scores showed approximately 50% aa identity with the ICEMlSymR7A RdfS, over approximately 55 aa for all of the putative RdfSs discovered in this study [Fig. 1]. No excisionase was found in the second Delftia acidovorans SPH-1 element. The location of this ORF is also of interest as usually excisionases are found close to the integrase gene in most ICEs particularly the SXT/R391 family [41].