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PlaB

Relationship

Family: PlaB

Block: X

Parent Family: Abhydrolase_6

Comment

Bacterial phospholipases. 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/dimerinterface, suggesting that these molecules stabilize the tetramer leading to enzyme inactivation.

Database

Interpro : No interpro

PIRSF : No PIRSF

Pdoc : No Pdoc

Pfam : PF12697 Abhydrolase_6

Prints : No Print

EC Number : No EC Number

Sequences

Peptide in Fasta
Nucleotide in Fasta
Alignment with Multalin Text only
Seed alignment with MAFFT No colour
Alignment with MAFFT No colour
Dendrogram The dnd file

References (4)

Title : A phospholipase B from Pseudomonas aeruginosa with activity towards endogenous phospholipids affects biofilm assembly - Weiler_2022_Biochim.Biophys.Acta.Mol.Cell.Biol.Lipids_1867_159101
Author(s) : Weiler AJ , Spitz O , Gudzuhn M , Schott-Verdugo SN , Kamel M , Thiele B , Streit WR , Kedrov A , Schmitt L , Gohlk H , Kovacic F , Gohlke H
Ref : Biochimica & Biophysica Acta Molecular & Cellular Biology Lipids , 1867 :159101 , 2022
Abstract : Weiler_2022_Biochim.Biophys.Acta.Mol.Cell.Biol.Lipids_1867_159101
ESTHER : Weiler_2022_Biochim.Biophys.Acta.Mol.Cell.Biol.Lipids_1867_159101
PubMedSearch : Weiler_2022_Biochim.Biophys.Acta.Mol.Cell.Biol.Lipids_1867_159101
PubMedID: 35063652
Gene_locus related to this paper: pseae-PA2927

Title : NAD(H)-mediated tetramerization controls the activity of Legionella pneumophila phospholipase PlaB - Diwo_2021_Proc.Natl.Acad.Sci.U.S.A_118_e2017046118
Author(s) : 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
Abstract : Diwo_2021_Proc.Natl.Acad.Sci.U.S.A_118_e2017046118
ESTHER : Diwo_2021_Proc.Natl.Acad.Sci.U.S.A_118_e2017046118
PubMedSearch : Diwo_2021_Proc.Natl.Acad.Sci.U.S.A_118_e2017046118
PubMedID: 34074754
Gene_locus related to this paper: legpn-i7i328

Title : Oligomerization Inhibits Legionella pneumophila PlaB Phospholipase A Activity - Kuhle_2014_J.Biol.Chem_289_18657
Author(s) : Kuhle K , Krausze J , Curth U , Rossle M , Heuner K , Lang C , Flieger A
Ref : Journal of Biological Chemistry , 289 :18657 , 2014
Abstract : Kuhle_2014_J.Biol.Chem_289_18657
ESTHER : Kuhle_2014_J.Biol.Chem_289_18657
PubMedSearch : Kuhle_2014_J.Biol.Chem_289_18657
PubMedID: 24811180
Gene_locus related to this paper: legpn-i7i328

Title : Phospholipase PlaB of Legionella pneumophila represents a novel lipase family: protein residues essential for lipolytic activity, substrate specificity, and hemolysis - Bender_2009_J.Biol.Chem_284_27185
Author(s) : Bender J , Rydzewski K , Broich M , Schunder E , Heuner K , Flieger A
Ref : Journal of Biological Chemistry , 284 :27185 , 2009
Abstract : Bender_2009_J.Biol.Chem_284_27185
ESTHER : Bender_2009_J.Biol.Chem_284_27185
PubMedSearch : Bender_2009_J.Biol.Chem_284_27185
PubMedID: 19640837
Gene_locus related to this paper: legpn-i7i328 , legsp-a3fmk8

Structures (2)

Genes Proteins in PlaB family (31)

Fragments of genes in PlaB family (2)

Structures in PlaB family (2)

Substrates in PlaB family (4)

Inhibitors in PlaB family (1)