(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Bacteria: NE > Proteobacteria: NE > Gammaproteobacteria: NE > Legionellales: NE > Legionellaceae: NE > Legionella: NE > Legionella pneumophila: NE
Warning: This entry is a compilation of different species or line or strain with more than 90% amino acid identity. You can retrieve all strain data
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) Legionella pneumophila str. Paris: N, E.
Legionella pneumophila str. Lens: N, E.
Legionella pneumophila subsp. pneumophila: N, E.
Legionella pneumophila subsp. pneumophila str. Philadelphia 1: N, E.
Legionella pneumophila str. Corby: N, E.
Legionella pneumophila 2300/99 Alcoy: N, E.
Legionella pneumophila 130b: N, E.
Legionella pneumophila serogroup 1: N, E.
Legionella pneumophila str. Leg01/11: N, E.
Legionella pneumophila str. Leg01/53: N, E.
Legionella pneumophila str. Leg01/20: N, E.
Legionella pneumophila subsp. pneumophila ATCC 43290: N, E.
Legionella pneumophila subsp. pneumophila str. Thunder Bay: N, E.
Legionella pneumophila subsp. pneumophila LPE509: N, E.
Legionella pneumophila str. 121004: N, E.
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA MGYSIINKNRSIKIILMIFIGITTFVKAYAYSPDTSNPIQINRSLTEVNS RHPGEVIVLIHGLMRTYVSMKPLKAYLEAQGYQVYLYKYPSARYNIQEHG VYLNQFITTILENNPAIKIHFVTHSLGGIIVREALSKLSQNQLKHVGYLI MLAPPNQGSKLAKLSIKLFPMISYFIKPLAELSSEQTSYVHRVPVPDIKM GIIAGRFDAKVPPDYARLQGQTEQVIINNTHTFIMYDSKVKKLVLSFLEK GKFE
Legionella pneumophila, the causative agent of Legionnaires' disease, replicates as an intracellular parasite of amoebae and persists in the environment as a free-living microbe. Here we have analyzed the complete genome sequences of L. pneumophila Paris (3,503,610 bp, 3,077 genes), an endemic strain that is predominant in France, and Lens (3,345,687 bp, 2,932 genes), an epidemic strain responsible for a major outbreak of disease in France. The L. pneumophila genomes show marked plasticity, with three different plasmids and with about 13% of the sequence differing between the two strains. Only strain Paris contains a type V secretion system, and its Lvh type IV secretion system is encoded by a 36-kb region that is either carried on a multicopy plasmid or integrated into the chromosome. Genetic mobility may enhance the versatility of L. pneumophila. Numerous genes encode eukaryotic-like proteins or motifs that are predicted to modulate host cell functions to the pathogen's advantage. The genome thus reflects the history and lifestyle of L. pneumophila, a human pathogen of macrophages that coevolved with fresh-water amoebae.
We present the genomic sequence of Legionella pneumophila, the bacterial agent of Legionnaires' disease, a potentially fatal pneumonia acquired from aerosolized contaminated fresh water. The genome includes a 45-kilobase pair element that can exist in chromosomal and episomal forms, selective expansions of important gene families, genes for unexpected metabolic pathways, and previously unknown candidate virulence determinants. We highlight the genes that may account for Legionella's ability to survive in protozoa, mammalian macrophages, and inhospitable environmental niches and that may define new therapeutic targets.
Title: Legionella pneumophila genes that encode lipase and phospholipase C activities Aragon V, Rossier O, Cianciotto NP Ref: Microbiology, 148:2223, 2002 : PubMed
Legionella pneumophila, the agent of Legionnaires' disease, is an intracellular parasite of aquatic protozoans and human macrophages. The type II protein secretion system of the Gram-negative Legionella organism promotes intracellular infection. A lipase activity and a p-nitrophenylphosphorylcholine (pNPPC) hydrolytic activity are two of the factors that are diminished in L. pneumophila type II secretion mutants. The Legionella lipase activity was found to include free fatty acid release from di- and triacylglycerol substrates, in addition to the previously reported cleavage of monoacylglycerol. In a number of other bacterial systems, the release of p-nitrophenol from pNPPC is due to a phospholipase C. In an attempt to identify exoproteins that potentiate intracellular infection, three genes were identified and mutated in L. pneumophila strain 130b that were predicted to encode either a secreted lipase or a phospholipase C. The first two genes, which were designated lipA and lipB, encoded proteins containing the lipase consensus sequence [LIV]-X-[LIVFY]-[LIVMST]-G-[HYWV]-S-X-G-[GSTAC]. Mutations in lipA in particular reduced supernatant activity against mono- and triacylglycerols. However, loss of lipA and/or lipB did not impair the ability of L. pneumophila to infect Hartmannella amoebae or U937 cell macrophages. The third L. pneumophila gene, which was denoted plcA, encoded a protein that was highly homologous with a phospholipase C from Pseudomonas fluorescens. Inactivation of plcA diminished secreted pNPPC hydrolase activity but did not influence Legionella infection of host cells. Taken together, these data indicate that L. pneumophila has multiple lipases and possibly several phospholipase C enzymes but that LipA, LipB and PlcA are not among those exoproteins required for optimal intracellular infection.
Legionella pneumophila Putative uncharacterized protein