PA1_SALTI
ID PA1_SALTI Reviewed; 289 AA.
AC P0A232; P37442; Q9L6N9;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=STY3602, t3340;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
CC -!- FUNCTION: Hydrolysis of phosphatidylcholine with phospholipase A2 (EC
CC 3.1.1.4) and phospholipase A1 (EC 3.1.1.32) activities. {ECO:0000250}.
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; AL513382; CAD07935.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO70868.1; -; Genomic_DNA.
DR RefSeq; NP_457794.1; NC_003198.1.
DR RefSeq; WP_001201692.1; NZ_WSUR01000033.1.
DR PDB; 7EZZ; X-ray; 2.76 A; A/B=33-289.
DR PDBsum; 7EZZ; -.
DR AlphaFoldDB; P0A232; -.
DR SMR; P0A232; -.
DR STRING; 220341.16504480; -.
DR EnsemblBacteria; AAO70868; AAO70868; t3340.
DR KEGG; stt:t3340; -.
DR KEGG; sty:STY3602; -.
DR PATRIC; fig|220341.7.peg.3671; -.
DR eggNOG; COG2829; Bacteria.
DR HOGENOM; CLU_045813_1_0_6; -.
DR OMA; WGGCRSV; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0052740; F:1-acyl-2-lysophosphatidylserine acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0052739; F:phosphatidylserine 1-acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008970; F:phospholipase A1 activity; IEA:UniProtKB-EC.
DR GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00541; OMPLA; 1.
DR Gene3D; 2.40.230.10; -; 1.
DR InterPro; IPR003187; PLipase_A1.
DR InterPro; IPR036541; PLipase_A1_sf.
DR PANTHER; PTHR40457; PTHR40457; 1.
DR Pfam; PF02253; PLA1; 1.
DR PRINTS; PR01486; PHPHLIPASEA1.
DR SUPFAM; SSF56931; SSF56931; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell outer membrane; Hydrolase; Lipid degradation;
KW Lipid metabolism; Membrane; Metal-binding; Signal; Transmembrane;
KW Transmembrane beta strand.
FT SIGNAL 1..20
FT /evidence="ECO:0000250"
FT CHAIN 21..289
FT /note="Phospholipase A1"
FT /id="PRO_0000021988"
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 HELIX 38..43
FT /evidence="ECO:0007829|PDB:7EZZ"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:7EZZ"
FT STRAND 59..66
FT /evidence="ECO:0007829|PDB:7EZZ"
FT TURN 70..75
FT /evidence="ECO:0007829|PDB:7EZZ"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:7EZZ"
FT STRAND 84..99
FT /evidence="ECO:0007829|PDB:7EZZ"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:7EZZ"
FT STRAND 106..118
FT /evidence="ECO:0007829|PDB:7EZZ"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:7EZZ"
FT STRAND 129..148
FT /evidence="ECO:0007829|PDB:7EZZ"
FT STRAND 151..164
FT /evidence="ECO:0007829|PDB:7EZZ"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:7EZZ"
FT STRAND 174..186
FT /evidence="ECO:0007829|PDB:7EZZ"
FT STRAND 189..200
FT /evidence="ECO:0007829|PDB:7EZZ"
FT HELIX 208..212
FT /evidence="ECO:0007829|PDB:7EZZ"
FT STRAND 214..223
FT /evidence="ECO:0007829|PDB:7EZZ"
FT STRAND 226..235
FT /evidence="ECO:0007829|PDB:7EZZ"
FT TURN 236..239
FT /evidence="ECO:0007829|PDB:7EZZ"
FT STRAND 240..254
FT /evidence="ECO:0007829|PDB:7EZZ"
FT STRAND 256..265
FT /evidence="ECO:0007829|PDB:7EZZ"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:7EZZ"
FT STRAND 275..285
FT /evidence="ECO:0007829|PDB:7EZZ"
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
