PA1_KLEPN
ID PA1_KLEPN Reviewed; 286 AA.
AC P37446;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 102.
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;
OS Klebsiella pneumoniae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573;
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).
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; X76901; CAA54223.1; -; Genomic_DNA.
DR PIR; B36971; B36971.
DR RefSeq; WP_004886777.1; NZ_UFBV01000019.1.
DR AlphaFoldDB; P37446; -.
DR SMR; P37446; -.
DR GeneID; 64297699; -.
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 3: Inferred from homology;
KW 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..286
FT /note="Phospholipase A1"
FT /id="PRO_0000021986"
FT TOPO_DOM 21..49
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 50..62
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TOPO_DOM 63..81
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 82..96
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TOPO_DOM 97..102
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 103..115
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TOPO_DOM 116..125
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 126..145
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TOPO_DOM 146..147
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 148..161
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TOPO_DOM 162..170
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 171..183
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TOPO_DOM 184..185
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 186..195
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TOPO_DOM 196..213
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 214..220
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TOPO_DOM 221..222
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 223..231
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TOPO_DOM 232..238
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 239..247
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TOPO_DOM 248..252
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 253..262
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TOPO_DOM 263..271
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 272..283
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TOPO_DOM 284..286
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT ACT_SITE 159
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 161
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 123
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 164
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 169
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 201
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /note="in monomeric form"
FT /evidence="ECO:0000250"
SQ SEQUENCE 286 AA; 32544 MW; 3E39F863085108A3 CRC64;
MRISLACLAA LCALPAGVMA QDASVHDKPA VRGSIIANLL QDHDNPFLLY PYESNYLLYT
WTSDLNKEAI RSYDWAENAR KDEVKFQLSL AFPLWRGILG DNSLLGASYT QKSWWQLSNS
KESAPFRETN YEPQLFLGFA TDYQFAGWTL RDIEMGYNHD SNGRSDPTSR SWNRLYARLM
AQNGNWLVEV KPWYVVGSTD DNPDITKYMG YYRLKVGYQL GEAILSAQGQ YNWNTGYGGA
ELGVSYPITK HVRAYTQIYS GYGESLIDYN FNQTRVGVGL MLNDLF
