(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 acide 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 subsp. pneumophila str. Philadelphia 1: N, E.
Legionella pneumophila subsp. pneumophila: N, E.
Legionella pneumophila str. Lens: N, E.
Legionella pneumophila str. Paris: 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 MAKIYNAPKPKYSGWEWFKFIAIRTVFPPVLLWDLIKIGANKLLGEWVSG LVLPAQNENFDDLAISDDTVSNYNEDDLICEKHDVITHDGAHLDTFEVRH RSQESIDPKYQKYIINLVGNGMCYEHIIDDIKEDSKALKANVIGFNLRGV GQSTGKAKSSEDLVADGIAQVQRLLDQGVSPQNITLKGHSLGAGVASLVA QHFHQLGQPINLFNSRSFSTITNFLVGHMRLERDEIGRAIGHKDSTVGTI LGWLAKPFIKFGVALAKWEINAGSAFKSVPEAYKDYIVVRSRKEIRGERI DDAVIPHYASIHKELASERHKKKAEIDEEIANLDDIIRKADPLAKPGLAN ARDALVQAREKIKSDRKMETDVQYANGHNSDWNALHNRSGKSAQTFFREF VQRTEADHAVKSIPEIN
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: Multiple substrates of the Legionella pneumophila Dot/Icm system identified by interbacterial protein transfer Luo ZQ, Isberg RR Ref: Proc Natl Acad Sci U S A, 101:841, 2004 : PubMed
Legionella pneumophila is an intracellular pathogen that multiplies in a specialized vacuole within host cells. Biogenesis of this vacuole requires the Dot/Icm type IV protein translocation system. By using a Cre/loxP-based protein translocation assay, we found that proteins translocated by the Dot/Icm complex across the host phagosomal membrane can also be transferred from one bacterial cell to another. The flexibility of this system allowed the identification of several families of proteins translocated by the Dot/Icm complex. When analyzed by immunofluorescence microscopy, a protein identified by this procedure, SidC, was shown to translocate across the phagosomal membranes to the cytoplasmic face of the L. pneumophila phagosome. The identification of large numbers of these substrates, and the fact that the absence of any one substrate rarely results in strong defects in intracellular growth, indicate that there is significant functional redundancy among the Dot/Icm translocation targets.