ID   PA1_PROVU               Reviewed;         289 AA.
AC   P37447;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   16-JUN-2009, entry version 48.
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=Phosphatidylcholine 1-acylhydrolase;
DE   AltName: Full=Outer membrane phospholipase A;
DE            Short=OM PLA;
DE   Flags: Precursor;
GN   Name=pldA;
OS   Proteus vulgaris.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Proteus.
OX   NCBI_TaxID=585;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=94131966; PubMed=8300539;
RA   Brok R.G.P.M., Brinkman E., van Boxtel R., Bekkers A.C.A.P.,
RA   Verheij H.M., Tommassen J.;
RT   "Molecular characterization of enterobacterial pldA genes encoding
RT   outer membrane phospholipase A.";
RL   J. Bacteriol. 176:861-870(1994).
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: Phosphatidylcholine + H(2)O = 2-
CC       acylglycerophosphocholine + a carboxylate.
CC   -!- CATALYTIC ACTIVITY: Phosphatidylcholine + H(2)O = 1-
CC       acylglycerophosphocholine + a carboxylate.
CC   -!- COFACTOR: Calcium.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane. Note=One of the very
CC       few enzymes located there.
CC   -!- SIMILARITY: Belongs to the phospholipase A1 family.
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DR   EMBL; X76902; CAA54224.1; -; Genomic_DNA.
DR   PIR; C36971; C36971.
DR   HSSP; P00631; 1QD6.
DR   SMR; P37447; 28-289.
DR   BRENDA; 3.1.1.32; 641.
DR   BRENDA; 3.1.1.4; 641.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008970; F:phospholipase A1 activity; IEA:EC.
DR   GO; GO:0004623; F:phospholipase A2 activity; IEA:EC.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR003187; PLA1.
DR   Gene3D; G3DSA:2.40.230.10; PLA1; 1.
DR   Pfam; PF02253; PLA1; 1.
DR   PRINTS; PR01486; PHPHLIPASEA1.
PE   3: Inferred from homology;
KW   Calcium; Cell membrane; Cell outer membrane; Hydrolase;
KW   Lipid degradation; Membrane; Signal.
FT   SIGNAL        1     20       By similarity.
FT   CHAIN        21    289       Phospholipase A1.
FT                                /FTId=PRO_0000021987.
FT   ACT_SITE    164    164       By similarity.
SQ   SEQUENCE   289 AA;  32945 MW;  D75516CFFB406997 CRC64;
     MRTGPGWLLA AAALPFFACA QEATIDKVHD TPAVRGSIIA NMLQEHDNPF TLYPYESNYL
     LYTYTSDLNK KAIESYNWSD NANKDEVKFQ LSLAFPLWRG ILGDNSLLGA SYTQRSWWQL
     SNTGESAPFR ETNYEPQLFL GFATDYSVGD WTLRDAEFGY NHQSNGRSDP TSRSWNRLYS
     RLMAQNGNWL VEVKPWYVIG DTSDNKNITK YMGYYQLKIG YQLGEAVLSA KGQYNWNTGY
     GGAELGVSYP ITKHVRFYTQ VYSGYGESLI DYDFNQTRVG MGVMLNDLF
//