ID PLA2_BEAB2 Reviewed; 190 AA. AC J4KMY5; DT 03-MAY-2023, integrated into UniProtKB/Swiss-Prot. DT 31-OCT-2012, sequence version 1. DT 28-JUN-2023, entry version 32. DE RecName: Full=Secretory phospholipase A2 {ECO:0000303|PubMed:35276754}; DE EC=3.1.1.4 {ECO:0000269|PubMed:35276754}; DE Flags: Precursor; GN Name=PLA2 {ECO:0000303|PubMed:35276754}; ORFNames=BBA_06333; OS Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus) OS (Tritirachium shiotae). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria. OX NCBI_TaxID=655819; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ARSEF 2860; RX PubMed=22761991; DOI=10.1038/srep00483; RA Xiao G., Ying S.-H., Zheng P., Wang Z.-L., Zhang S., Xie X.-Q., Shang Y., RA St Leger R.J., Zhao G.-P., Wang C., Feng M.-G.; RT "Genomic perspectives on the evolution of fungal entomopathogenicity in RT Beauveria bassiana."; RL Sci. Rep. 2:483-483(2012). RN [2] RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, CATALYTIC ACTIVITY, RP BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION PHENOTYPE. RX PubMed=35276754; DOI=10.1111/1744-7917.13029; RA Deng J., Lu Z., Wang H., Li N., Song G., Zhu Q., Sun J., Zhang Y.; RT "A secretory phospholipase A2 of a fungal pathogen contributes to lipid RT droplet homeostasis, assimilation of insect-derived lipids, and repression RT of host immune responses."; RL Insect Sci. 29:1685-1702(2022). CC -!- FUNCTION: Secretory phospholipase that catalyzes the calcium-dependent CC hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides CC (PubMed:35276754). Increases the ability to utilize insect-derived CC nutrients and lipids, and promotes lipid dropplets accumulation CC (PubMed:35276754). Plays a role in virulence, including more efficient CC penetration of the insect cuticle and evasion of host immune response CC by repressing the expression of host immunity genes (PubMed:35276754). CC {ECO:0000269|PubMed:35276754}. 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:0000269|PubMed:35276754}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802; CC Evidence={ECO:0000269|PubMed:35276754}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000305|PubMed:35276754}; CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000305|PubMed:35276754}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.56 mM for phosphatidyl-choline {ECO:0000269|PubMed:35276754}; CC pH dependence: CC Optimum pH is 7.0-11.0. {ECO:0000269|PubMed:35276754}; CC Temperature dependence: CC Optimum temperature is 35 degrees Celsius. CC {ECO:0000269|PubMed:35276754}; CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:35276754}. CC Secreted {ECO:0000269|PubMed:35276754}. CC -!- INDUCTION: Expression is dramatically induced in the presence of insect CC hemolymph as well as by lipids (PubMed:35276754). In addition, is also CC up-regulated in cultures containing insect cuticle and under conditions CC of nutrient starvation (PubMed:35276754). CC {ECO:0000269|PubMed:35276754}. CC -!- DISRUPTION PHENOTYPE: Decreases the ability to penetrate the host CC cuticle and impairs the repression of host immunity genes. CC {ECO:0000269|PubMed:35276754}. CC -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JH725167; EJP64764.1; -; Genomic_DNA. DR RefSeq; XP_008599652.1; XM_008601430.1. DR AlphaFoldDB; J4KMY5; -. DR SMR; J4KMY5; -. DR GeneID; 19889345; -. DR HOGENOM; CLU_053014_1_0_1; -. DR InParanoid; J4KMY5; -. DR Proteomes; UP000002762; Unassembled WGS sequence. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004623; F:phospholipase A2 activity; IEA:InterPro. DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro. 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; Phospholipase A2 domain; 1. DR InterPro; IPR036444; PLipase_A2_dom_sf. DR InterPro; IPR015141; PLipase_A2_prok/fun. DR PANTHER; PTHR40787; SECRETED PROTEIN; 1. DR PANTHER; PTHR40787:SF2; SECRETED PROTEIN; 1. DR Pfam; PF09056; Phospholip_A2_3; 1. DR SUPFAM; SSF48619; Phospholipase A2, PLA2; 1. PE 1: Evidence at protein level; KW Calcium; Disulfide bond; Hydrolase; Lipid degradation; Lipid droplet; KW Lipid metabolism; Metal-binding; Reference proteome; Secreted; Signal; KW Virulence. FT SIGNAL 1..15 FT /evidence="ECO:0000255" FT CHAIN 16..190 FT /note="Secretory phospholipase A2" FT /id="PRO_5012361776" FT ACT_SITE 81 FT /evidence="ECO:0000250|UniProtKB:P00593" FT BINDING 65 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:P00593" FT BINDING 82 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:P00593" FT DISULFID 62..78 FT /evidence="ECO:0000250|UniProtKB:P04054" SQ SEQUENCE 190 AA; 21498 MW; 4BA4B74AF0871E69 CRC64; MKLAYFSSLL PLALAAPASV VDPREPKEDI TDRYLFSTPL PTFLEYREKE NPDSLDWTSD GCTHASNNPF GFPFEPACQR HDFGYRNYQA QTRFESDSRY RIDLNFYNDM IFQCTDVSAL RSCHGLADVY YAGVRMFGGF AKRDEMGAVV ASATDPKESA EDLIAVYYTA LQEYHQAVKA DQADGLLPRL //