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Literature summary extracted from

  • Aurass, P.; Schlegel, M.; Metwally, O.; Harding, C.R.; Schroeder, G.N.; Frankel, G.; Flieger, A.
    The Legionella pneumophila Dot/Icm-secreted effector PlcC/CegC1 together with PlcA and PlcB promotes virulence and belongs to a novel zinc metallophospholipase C family present in bacteria and fungi (2013), J. Biol. Chem., 288, 11080-11092.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.4.3 gene lpg0012 or plcC, DNA and amino acid sequence determination and analysis, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain DH5alpha. Expression of Strep-tagged enzyme mutants H179N and S336A does not yield any detectable protein Legionella pneumophila

Protein Variants

EC Number Protein Variants Comment Organism
3.1.4.3 D251V site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme Legionella pneumophila
3.1.4.3 D314V site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme Legionella pneumophila
3.1.4.3 D63V site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme Legionella pneumophila
3.1.4.3 E286A site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme Legionella pneumophila
3.1.4.3 F167A site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme Legionella pneumophila
3.1.4.3 F244A site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme Legionella pneumophila
3.1.4.3 F253A site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme Legionella pneumophila
3.1.4.3 H166N site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme Legionella pneumophila
3.1.4.3 H179N site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme Legionella pneumophila
3.1.4.3 H247N site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme Legionella pneumophila
3.1.4.3 H257N site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme Legionella pneumophila
3.1.4.3 H284N site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme Legionella pneumophila
3.1.4.3 H409N site-directed mutagenesis, the mutant enzyme shows similar catalytic activity as the wild-type enzyme Legionella pneumophila
3.1.4.3 additional information construction of enzyme knock-out mutants, of PlcC alone, or double PlcC/PlcA or PlcC/PlcB and triple PlcC/PlcA/PlcB mutants. Complementation of plcC knock-out mutants with wild-type plcC in trans restores the cell-associated enzyme activity defect Legionella pneumophila
3.1.4.3 R265Q site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme Legionella pneumophila
3.1.4.3 R326Q site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme Legionella pneumophila
3.1.4.3 R365Q site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme Legionella pneumophila
3.1.4.3 S336A site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme Legionella pneumophila
3.1.4.3 Y156A site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme Legionella pneumophila

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.4.3 EDTA
-
 Legionella pneumophila

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.4.3 extracellular IVB Dot/Icm secretion type. The secreted enzyme activity depends upon an intact type II secretion system Legionella pneumophila
-
-
3.1.4.3 additional information the enzyme sequence contains no signal peptide Legionella pneumophila
-
-
3.1.4.3 type IV secretion system complex
-
 Legionella pneumophila 43684
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.4.3 Zn2+ activates Legionella pneumophila

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.4.3 60090
-
 x * 60090, sequence calculation Legionella pneumophila

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.4.3 phosphatidylcholine + H2O Legionella pneumophila the enzyme shows cell-associated phosphatidylcholine-specific phospholipase C activity in vivo 1,2-sn-diacylglycerol + phosphocholine
-
 ?
3.1.4.3 phosphatidylcholine + H2O Legionella pneumophila JR32 the enzyme shows cell-associated phosphatidylcholine-specific phospholipase C activity in vivo 1,2-sn-diacylglycerol + phosphocholine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.4.3 Legionella pneumophila Q5ZZJ8 gene lpg0012 or plcC
-
3.1.4.3 Legionella pneumophila JR32 Q5ZZJ8 gene lpg0012 or plcC
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.4.3 additional information the recombinant enzyme hydrolyzes a broad phospholipid spectrum, including phosphatidylcholine, phosphatidylglycerol, and phosphatidylinositol, broad substrate preference Legionella pneumophila ?
-
 ?
3.1.4.3 additional information the recombinant enzyme hydrolyzes a broad phospholipid spectrum, including phosphatidylcholine, phosphatidylglycerol, and phosphatidylinositol, broad substrate preference Legionella pneumophila JR32 ?
-
 ?
3.1.4.3 phosphatidylcholine + H2O
-
 Legionella pneumophila 1,2-sn-diacylglycerol + phosphocholine
-
 ?
3.1.4.3 phosphatidylcholine + H2O the enzyme shows cell-associated phosphatidylcholine-specific phospholipase C activity in vivo Legionella pneumophila 1,2-sn-diacylglycerol + phosphocholine
-
 ?
3.1.4.3 phosphatidylcholine + H2O
-
 Legionella pneumophila JR32 1,2-sn-diacylglycerol + phosphocholine
-
 ?
3.1.4.3 phosphatidylcholine + H2O the enzyme shows cell-associated phosphatidylcholine-specific phospholipase C activity in vivo Legionella pneumophila JR32 1,2-sn-diacylglycerol + phosphocholine
-
 ?
3.1.4.3 phosphatidylglycerol + H2O
-
 Legionella pneumophila 1,2-sn-diacylglycerol + sn-glycerol-3-phosphate
-
 ?
3.1.4.3 phosphatidylglycerol + H2O
-
 Legionella pneumophila JR32 1,2-sn-diacylglycerol + sn-glycerol-3-phosphate
-
 ?
3.1.4.3 phosphatidylinositol + H2O
-
 Legionella pneumophila 1,2-sn-diacylglycerol + phosphoinositol
-
 ?
3.1.4.3 phosphatidylinositol + H2O
-
 Legionella pneumophila JR32 1,2-sn-diacylglycerol + phosphoinositol
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.4.3 ? x * 60090, sequence calculation Legionella pneumophila

Synonyms

EC Number Synonyms Comment Organism
3.1.4.3 CegC1
-
 Legionella pneumophila
3.1.4.3 Dot/Icm-injected effector
-
 Legionella pneumophila
3.1.4.3 Lpg0012
-
 Legionella pneumophila
3.1.4.3 PC-PLC
-
 Legionella pneumophila
3.1.4.3 phosphatidylcholine-specific phospholipase C
-
 Legionella pneumophila
3.1.4.3 plcC
-
 Legionella pneumophila
3.1.4.3 PlcC/CegC1
-
 Legionella pneumophila

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.4.3 37
-
 assay at Legionella pneumophila

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.4.3 7.5
-
 assay at Legionella pneumophila

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.1.4.3 Legionella pneumophila sequence calculation
-
 6.55

Expression

EC Number Organism Comment Expression
3.1.4.3 Legionella pneumophila the enzyme is upregulated during infection of Acanthamoeba castellanii amoebae and macrophages up

General Information

EC Number General Information Comment Organism
3.1.4.3 evolution the enzyme belongs to a distinct zinc metallophospholipase C family present in bacteria and fungi Legionella pneumophila
3.1.4.3 malfunction enzyme knock-out mutants of PlcC show abolished enzyme activity. Complementation of plcC knock-out mutants with wild-type plcC in trans restores the cell-associated enzyme activity defect Legionella pneumophila
3.1.4.3 additional information the fifteen conserved amino acids Asp63, Tyr156, His166, Phe167, Phe244, His247, Asp251, Phe253, Arg265, His257, His284, Glu286, Asp314, Arg326, and Arg385 are essential for enzyme activity Legionella pneumophila
3.1.4.3 physiological function the enzyme, phosphatidylcholine-specific phospholipase C or effector PlcC/CegC1, together with Zn2+-dependent enzymes PlcA and PlcB, exhibiting phosphatidylglycerol hydrolysis activity, promote virulence, e.g. in Acanthamoeba castellanii amoebae and human U937 cells or in Galleria mellonella larvae, but are not essential. The enzyme is CpxR-co-regulated Legionella pneumophila