ID   PA1_SALTY               Reviewed;         289 AA.
AC   P0A231; P37442; Q9L6N9;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   02-SEP-2026, entry version 112.
DE   RecName: Full=Phospholipase A1;
DE            EC=3.1.1.32;
DE            EC=3.1.1.4;
DE   AltName: Full=Detergent-resistant phospholipase A;
DE            Short=DR-phospholipase A;
DE   AltName: Full=Outer membrane phospholipase A;
DE            Short=OM PLA;
DE   AltName: Full=Phosphatidylcholine 1-acylhydrolase;
DE   Flags: Precursor;
GN   Name=pldA; OrderedLocusNames=STM3957; ORFNames=STMD1.33;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8300539; DOI=10.1128/jb.176.3.861-870.1994;
RA   Brok R.G.P.M., Brinkman E., van Boxtel R., Bekkers A.C.A.P., Verheij H.M.,
RA   Tommassen J.;
RT   "Molecular characterization of enterobacterial pldA genes encoding outer
RT   membrane phospholipase A.";
RL   J. Bacteriol. 176:861-870(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
CC   -!- FUNCTION: Hydrolysis of phosphatidylcholine with phospholipase A2
CC       (EC 3.1.1.4) and phospholipase A1 (EC 3.1.1.32) activities.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-
CC         glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC         ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32;
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   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 1 Ca(2+) ion per monomer. In the dimeric form the Ca(2+) is
CC       bound by different amino acids with binding of each Ca(2+) shared with
CC       ligands coming from each monomer. The Ca(2+) ion may have a role in
CC       catalysis. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer; dimerization is reversible, and the dimeric form is
CC       the active one. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}. Note=One of the very few enzymes
CC       located there. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the phospholipase A1 family. {ECO:0000305}.
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DR   EMBL; X76900; CAA54222.1; -; Genomic_DNA.
DR   EMBL; AF233324; AAF33435.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL22801.1; -; Genomic_DNA.
DR   PIR; A36971; A36971.
DR   RefSeq; NP_462842.1; NC_003197.2.
DR   RefSeq; WP_001201692.1; NC_003197.2.
DR   AlphaFoldDB; P0A231; -.
DR   SMR; P0A231; -.
DR   STRING; 99287.STM3957; -.
DR   PaxDb; 99287-STM3957; -.
DR   GeneID; 1255483; -.
DR   KEGG; stm:STM3957; -.
DR   PATRIC; fig|99287.12.peg.4175; -.
DR   HOGENOM; CLU_045813_1_0_6; -.
DR   OMA; DVRWGGC; -.
DR   PhylomeDB; P0A231; -.
DR   BioCyc; SENT99287:STM3957-MONOMER; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0009279; C:cell outer membrane; IBA:GO_Central.
DR   GO; GO:0004623; F:A2-type glycerophospholipase activity; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0008970; F:glycerophospholipid phospholipase A1 activity; IEA:UniProtKB-EC.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   CDD; cd00541; OMPLA; 1.
DR   FunFam; 2.40.230.10:FF:000001; Phospholipase A(1); 1.
DR   Gene3D; 2.40.230.10; Phospholipase A1; 1.
DR   InterPro; IPR003187; PLipase_A1.
DR   InterPro; IPR036541; PLipase_A1_sf.
DR   NCBIfam; NF008031; PRK10763.1; 1.
DR   PANTHER; PTHR40457; PHOSPHOLIPASE A1; 1.
DR   PANTHER; PTHR40457:SF1; PHOSPHOLIPASE A1; 1.
DR   Pfam; PF02253; PLA1; 1.
DR   PRINTS; PR01486; PHPHLIPASEA1.
DR   SUPFAM; SSF56931; Outer membrane phospholipase A (OMPLA); 1.
PE   3: Inferred from homology;
KW   Calcium; Cell outer membrane; Hydrolase; Lipid degradation;
KW   Lipid metabolism; Membrane; Metal-binding; Reference proteome; Signal;
KW   Transmembrane; Transmembrane beta strand.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000250"
FT   CHAIN           21..289
FT                   /note="Phospholipase A1"
FT                   /id="PRO_0000021989"
FT   TOPO_DOM        21..52
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        53..65
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        66..84
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        85..99
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        100..105
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        106..118
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        119..128
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        129..148
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        149..150
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        151..164
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        165..173
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        174..186
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        187..188
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        189..198
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        199..216
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        217..223
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        224..225
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        226..234
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        235..241
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        242..250
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        251..255
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        256..265
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        266..274
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        275..286
FT                   /note="Beta stranded"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        287..289
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        162
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        164
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         126
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /note="in dimeric form"
FT                   /evidence="ECO:0000250"
FT   BINDING         167
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /note="in dimeric form"
FT                   /evidence="ECO:0000250"
FT   BINDING         172
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /note="in dimeric form"
FT                   /evidence="ECO:0000250"
FT   BINDING         204
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /note="in monomeric form"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        155
FT                   /note="D -> H (in Ref. 1; CAA54222)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        174
FT                   /note="S -> T (in Ref. 1; CAA54222)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   289 AA;  32967 MW;  DA97F5E1651C49C6 CRC64;
     MRAILRGLLP ATLLPLAAYA QEATIKEVHD APAVRGSIIA NMLQEHDNPF TLYPYDTNYL
     IYTNTSDLNK EAISTYNWSE NARKDEVKFQ LSLAFPLWRG ILGPNSVLGA SYTQKSWWQL
     SNSKESSPFR ETNYEPQLFL GFATDYRFAG WTLRDVEMGY NHDSNGRSDP TSRSWNRLYT
     RLMAENGNWL VEVKPWYVIG STDDNPDITK YMGYYQLKIG YHLGEAVLSA KGQYNWNTGY
     GGAEVGLSYP VTKHVRLYTQ VYSGYGESLI DYNFNQTRVG VGVMLNDIF
//