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Phospholipase A1 (EC 3.1.1.32) (EC 3.1.1.4) (Detergent-resistant phospholipase A) (DR-phospholipase A) (Outer membrane phospholipase A) (OM PLA) (Phosphatidylcholine 1-acylhydrolase)

 PA1_SALTY               Reviewed;         289 AA.
P0A231; P37442; Q9L6N9;
01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2005, sequence version 1.
05-DEC-2018, entry version 86.
RecName: Full=Phospholipase A1;
EC=3.1.1.32;
EC=3.1.1.4;
AltName: Full=Detergent-resistant phospholipase A;
Short=DR-phospholipase A;
AltName: Full=Outer membrane phospholipase A;
Short=OM PLA;
AltName: Full=Phosphatidylcholine 1-acylhydrolase;
Flags: Precursor;
Name=pldA; OrderedLocusNames=STM3957; ORFNames=STMD1.33;
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Salmonella.
NCBI_TaxID=99287;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8300539; DOI=10.1128/jb.176.3.861-870.1994;
Brok R.G.P.M., Brinkman E., van Boxtel R., Bekkers A.C.A.P.,
Verheij H.M., Tommassen J.;
"Molecular characterization of enterobacterial pldA genes encoding
outer membrane phospholipase A.";
J. Bacteriol. 176:861-870(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=LT2 / SGSC1412 / ATCC 700720;
PubMed=11677609; DOI=10.1038/35101614;
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M.,
Waterston R., Wilson R.K.;
"Complete genome sequence of Salmonella enterica serovar Typhimurium
LT2.";
Nature 413:852-856(2001).
-!- FUNCTION: Hydrolysis of phosphatidylcholine with phospholipase A2
(EC 3.1.1.4) and phospholipase A1 (EC 3.1.1.32) activities.
-!- CATALYTIC ACTIVITY:
Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-
acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+);
Xref=Rhea:RHEA:18689, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:57875;
EC=3.1.1.32;
-!- CATALYTIC ACTIVITY:
Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-
acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+);
Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168;
EC=3.1.1.4;
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
Note=Binds 1 Ca(2+) ion per monomer. In the dimeric form the
Ca(2+) is bound by different amino acids with binding of each
Ca(2+) shared with ligands coming from each monomer. The Ca(2+)
ion may have a role in catalysis. {ECO:0000250};
-!- SUBUNIT: Homodimer; dimerization is reversible, and the dimeric
form is the active one. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Multi-
pass membrane protein {ECO:0000250}. Note=One of the very few
enzymes located there. {ECO:0000250}.
-!- SIMILARITY: Belongs to the phospholipase A1 family. {ECO:0000305}.
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EMBL; X76900; CAA54222.1; -; Genomic_DNA.
EMBL; AF233324; AAF33435.1; -; Genomic_DNA.
EMBL; AE006468; AAL22801.1; -; Genomic_DNA.
PIR; A36971; A36971.
RefSeq; NP_462842.1; NC_003197.2.
RefSeq; WP_001201692.1; NC_003197.2.
ProteinModelPortal; P0A231; -.
SMR; P0A231; -.
STRING; 99287.STM3957; -.
PaxDb; P0A231; -.
PRIDE; P0A231; -.
EnsemblBacteria; AAL22801; AAL22801; STM3957.
GeneID; 1255483; -.
KEGG; stm:STM3957; -.
PATRIC; fig|99287.12.peg.4175; -.
eggNOG; ENOG4105HDD; Bacteria.
eggNOG; COG2829; LUCA.
HOGENOM; HOG000288150; -.
KO; K01058; -.
OMA; WGGCRSV; -.
BioCyc; SENT99287:STM3957-MONOMER; -.
Proteomes; UP000001014; Chromosome.
GO; GO:0045203; C:integral component of cell outer membrane; IBA:GO_Central.
GO; GO:0052740; F:1-acyl-2-lysophosphatidylserine acylhydrolase activity; IEA:UniProtKB-EC.
GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
GO; GO:0052739; F:phosphatidylserine 1-acylhydrolase activity; IEA:UniProtKB-EC.
GO; GO:0008970; F:phospholipase A1 activity; IEA:UniProtKB-EC.
GO; GO:0004623; F:phospholipase A2 activity; IBA:GO_Central.
GO; GO:0102567; F:phospholipase A2 activity (consuming 1,2-dipalmitoylphosphatidylcholine); IEA:UniProtKB-EC.
GO; GO:0102568; F:phospholipase A2 activity consuming 1,2-dioleoylphosphatidylethanolamine); IEA:UniProtKB-EC.
GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
CDD; cd00541; OMPLA; 1.
Gene3D; 2.40.230.10; -; 1.
InterPro; IPR003187; PLipase_A1.
InterPro; IPR036541; PLipase_A1_sf.
PANTHER; PTHR40457; PTHR40457; 1.
Pfam; PF02253; PLA1; 1.
PRINTS; PR01486; PHPHLIPASEA1.
SUPFAM; SSF56931; SSF56931; 1.
3: Inferred from homology;
Calcium; Cell outer membrane; Complete proteome; Hydrolase;
Lipid degradation; Lipid metabolism; Membrane; Metal-binding;
Reference proteome; Signal; Transmembrane; Transmembrane beta strand.
SIGNAL 1 20 {ECO:0000250}.
CHAIN 21 289 Phospholipase A1.
/FTId=PRO_0000021989.
TOPO_DOM 21 52 Periplasmic. {ECO:0000250}.
TRANSMEM 53 65 Beta stranded. {ECO:0000250}.
TOPO_DOM 66 84 Extracellular. {ECO:0000250}.
TRANSMEM 85 99 Beta stranded. {ECO:0000250}.
TOPO_DOM 100 105 Periplasmic. {ECO:0000250}.
TRANSMEM 106 118 Beta stranded. {ECO:0000250}.
TOPO_DOM 119 128 Extracellular. {ECO:0000250}.
TRANSMEM 129 148 Beta stranded. {ECO:0000250}.
TOPO_DOM 149 150 Periplasmic. {ECO:0000250}.
TRANSMEM 151 164 Beta stranded. {ECO:0000250}.
TOPO_DOM 165 173 Extracellular. {ECO:0000250}.
TRANSMEM 174 186 Beta stranded. {ECO:0000250}.
TOPO_DOM 187 188 Periplasmic. {ECO:0000250}.
TRANSMEM 189 198 Beta stranded. {ECO:0000250}.
TOPO_DOM 199 216 Extracellular. {ECO:0000250}.
TRANSMEM 217 223 Beta stranded. {ECO:0000250}.
TOPO_DOM 224 225 Periplasmic. {ECO:0000250}.
TRANSMEM 226 234 Beta stranded. {ECO:0000250}.
TOPO_DOM 235 241 Extracellular. {ECO:0000250}.
TRANSMEM 242 250 Beta stranded. {ECO:0000250}.
TOPO_DOM 251 255 Periplasmic. {ECO:0000250}.
TRANSMEM 256 265 Beta stranded. {ECO:0000250}.
TOPO_DOM 266 274 Extracellular. {ECO:0000250}.
TRANSMEM 275 286 Beta stranded. {ECO:0000250}.
TOPO_DOM 287 289 Periplasmic. {ECO:0000250}.
ACT_SITE 162 162 Proton acceptor. {ECO:0000250}.
ACT_SITE 164 164 Nucleophile. {ECO:0000250}.
METAL 126 126 Calcium 1; via carbonyl oxygen; in
dimeric form. {ECO:0000250}.
METAL 167 167 Calcium 2; via carbonyl oxygen; in
dimeric form. {ECO:0000250}.
METAL 172 172 Calcium 2; in dimeric form.
{ECO:0000250}.
METAL 204 204 Calcium 3; in monomeric form.
{ECO:0000250}.
CONFLICT 155 155 D -> H (in Ref. 1; CAA54222).
{ECO:0000305}.
CONFLICT 174 174 S -> T (in Ref. 1; CAA54222).
{ECO:0000305}.
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


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