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Gene_locus Report for: legpn-i7i328

Legionella pneumophila subsp. pneumophila Legionella drancourtii, Phospholipase LpPlaB

Comment
Legionella pneumophila possesses a major cell-associated hemolytic phospholipase A (PlaB) which shares no homology to described phospholipases. PlaB preferentially hydrolyzes long-chain fatty acid substrates containing 12 or more carbon atoms. PlaB shows concentration-dependent phospholipase inactivation by tetramerization which may be a mechanism for self-protection. (See Papers Bender et al. 2009 and Kuhle et al. 2014.). The tetramer is a dimer of identical dimers. Diwo et al. found in the structure eight NAD(H) molecules at the dimer/dimer interface, suggesting that these molecules stabilize the tetramer leading to enzyme inactivation (Diwo et al.).The N-Terminal Phospholipase domain is a typical alpha/beta-Hydrolase extended by the non canonical two-stranded beta-sheets beta-6/beta-7 and beta-9/beta-10.. Other strains: Legionella pneumophila Paris; Leg01/20; Leg01/11; Leg01/53; 121004; Thunder Bay; Philadelphia 1 / ATCC 33152 / DSM 7513; Lens; Legionella drancourtii LLAP12; ATCC 43290; serogroup 1 (strain 2300/99 Alcoy); Corby; LPE509


Relationship
Family|PlaB
Block| X
Position in NCBI Life Tree|Legionella pneumophila
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.)
> cellular organisms: N E > Bacteria: N E > Proteobacteria: N E > Gammaproteobacteria: N E > Legionellales: N E > Legionellaceae: N E > Legionella: N E > Legionella pneumophila: N E
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


Molecular evidence
Database
Sequence
Graphical view for this peptide sequence: legpn-i7i328
Colored MSA for PlaB (raw)
MIVIFVHGWSVTHTNTYGELPQWLENQSKQGKLDIQVGNIYLGRYISFDD
TVTVDDIARAFDQAVRDEIADKLRDGQRFACITHSTGGPIVRKWMDLYFK
NNLAKCPLSHLIMLAPANHGSALAQLGKSRLGRIKSFFEGIEPGKCVLDW
LELGSDMSWQLNESWLDYDCTANGVYSFVLTGQKIDRQFYDAVNSYTGES
GSDGVVRVAATNMNYSLLKLHQEGDNGESLVVAKMTRTQPMAFGVLPGLS
HSGKNIGIIRSITMANAATHPTAIWILRCLQVKSRDSYNKLVKELDNITK
ETQKNEHKEFVKTLVFTREYITNRYSMIIFRLIDDRGNHLIDYDLYLTAG
PQYSEQALPAGFFVDRQRNLNNRGKLTYFLDYDIMEGGINTPKMQGNLGF
RVKAYPESSDQALAYYRLLDFHSSLADIHKILHPNETVMVEIMLQRRVDR
TVFRISNNLTPAKISGKPTGKKID
Legend This 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

MIVIFVHGWSVTHTNTYGELPQWLENQSKQGKLDIQVGNIYLGRYISFDD
TVTVDDIARAFDQAVRDEIADKLRDGQRFACITHSTGGPIVRKWMDLYFK
NNLAKCPLSHLIMLAPANHGSALAQLGKSRLGRIKSFFEGIEPGKCVLDW
LELGSDMSWQLNESWLDYDCTANGVYSFVLTGQKIDRQFYDAVNSYTGES
GSDGVVRVAATNMNYSLLKLHQEGDNGESLVVAKMTRTQPMAFGVLPGLS
HSGKNIGIIRSITMANAATHPTAIWILRCLQVKSRDSYNKLVKELDNITK
ETQKNEHKEFVKTLVFTREYITNRYSMIIFRLIDDRGNHLIDYDLYLTAG
PQYSEQALPAGFFVDRQRNLNNRGKLTYFLDYDIMEGGINTPKMQGNLGF
RVKAYPESSDQALAYYRLLDFHSSLADIHKILHPNETVMVEIMLQRRVDR
TVFRISNNLTPAKISGKPTGKKID


References
8 more
    Title: NAD(H)-mediated tetramerization controls the activity of Legionella pneumophila phospholipase PlaB
    Diwo M, Michel W, Aurass P, Kuhle-Keindorf K, Pippel J, Krausze J, Wamp S, Lang C, Blankenfeldt W, Flieger A
    Ref: Proc Natl Acad Sci U S A, 118:, 2021 : PubMed

            

    Title: Oligomerization Inhibits Legionella pneumophila PlaB Phospholipase A Activity
    Kuhle K, Krausze J, Curth U, Rossle M, Heuner K, Lang C, Flieger A
    Ref: Journal of Biological Chemistry, 289:18657, 2014 : PubMed

            

    Title: Cloning and characterization of the gene encoding the major cell-associated phospholipase A of Legionella pneumophila, plaB, exhibiting hemolytic activity
    Flieger A, Rydzewski K, Banerji S, Broich M, Heuner K
    Ref: Infect Immun, 72:2648, 2004 : PubMed

            


Other Papers


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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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