PLA2_WALAE
ID PLA2_WALAE Reviewed; 30 AA.
AC P0DQD1;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 13-FEB-2019, sequence version 1.
DT 03-AUG-2022, entry version 8.
DE RecName: Full=Non-toxic phospholiapse A2 {ECO:0000303|PubMed:29885399};
DE Short=WaPLA2 {ECO:0000303|PubMed:29885399};
DE Short=svPLA2 {ECO:0000305};
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase {ECO:0000305};
DE EC=3.1.1.4 {ECO:0000305};
DE Flags: Fragment;
OS Walterinnesia aegyptia (Desert black snake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Walterinnesia.
OX NCBI_TaxID=64182;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, SUBUNIT, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=29885399; DOI=10.1016/j.ijbiomac.2018.06.024;
RA Ben Bacha A., Alonazi M.A., Elshikh M.S., Karray A.;
RT "A novel bactericidal homodimeric PLA2 group-I from Walterinnesia aegyptia
RT venom.";
RL Int. J. Biol. Macromol. 117:1140-1146(2018).
CC -!- FUNCTION: Relatively highly potent phospholipase A2 that displays
CC potent antimicrobial and hemolytic activities. It does not show
CC cytotoxic effects on the three human cell lines tested. PLA2 catalyzes
CC the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-
CC phosphoglycerides. It shows similar potencies on both Gram-negative and
CC Gram-positive bacteria: B.cereus (MIC>9 ug/ml), B.subtilis (MIC>12
CC ug/ml), E.faecalis (MIC>7 ug/ml), S.epidermidis (MIC>12 ug/ml),
CC S.aureux (MIC>5 ug/ml), E.coli (MIC>7 ug/ml), K.pneumonia (MIC>8
CC ug/ml), P.aeruginosa (MIC>10 ug/ml), and S.enteric (MIC>9 ug/ml). It
CC also shows antifungal activities: A.niger (MIC>15 ug/ml), B.cinerea
CC (MIC>12 ug/ml), F.solani (MIC>15 ug/ml), and P.digitatum (MIC>10
CC ug/ml). {ECO:0000269|PubMed:29885399}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4;
CC Evidence={ECO:0000305};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:29885399};
CC -!- ACTIVITY REGULATION: Enzymatic activity is diminished by Cd(2+) and
CC Hg(2+). {ECO:0000269|PubMed:29885399}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=2100 umol/min/mg enzyme {ECO:0000269|PubMed:29885399};
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:29885399};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius.
CC {ECO:0000269|PubMed:29885399};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:29885399}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29885399}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:29885399}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:29885399}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC {ECO:0000305}.
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DR AlphaFoldDB; P0DQD1; -.
DR SMR; P0DQD1; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR Gene3D; 1.20.90.10; -; 1.
DR InterPro; IPR001211; PLipase_A2.
DR InterPro; IPR036444; PLipase_A2_dom_sf.
DR PRINTS; PR00389; PHPHLIPASEA2.
DR SUPFAM; SSF48619; SSF48619; 1.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Calcium; Cytolysis; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hemolysis; Hydrolase; Lipid degradation;
KW Lipid metabolism; Metal-binding; Secreted.
FT CHAIN 1..>30
FT /note="Non-toxic phospholiapse A2"
FT /evidence="ECO:0000269|PubMed:29885399"
FT /id="PRO_0000446236"
FT BINDING 26
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9DF52"
FT BINDING 28
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9DF52"
FT BINDING 30
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9DF52"
FT DISULFID 17
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:A6MEY4"
FT NON_TER 30
SQ SEQUENCE 30 AA; 3351 MW; C7DF10A88B8ABF10 CRC64;
NLYQFKNMVQ CVGTQLCVAY VKYGCYCGPG
