PA1_ECOLI
ID PA1_ECOLI Reviewed; 289 AA.
AC P0A921; P00631; Q2M8C6;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 121.
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 Short=OMPLA;
DE AltName: Full=Phosphatidylcholine 1-acylhydrolase;
DE Flags: Precursor;
GN Name=pldA; OrderedLocusNames=b3821, JW3794;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 21-30.
RC STRAIN=K12;
RX PubMed=6397464; DOI=10.1093/oxfordjournals.jbchem.a134997;
RA Homma H., Kobayashi T., Chiba N., Karasawa K., Mizushima H., Kudo I.,
RA Inoue K., Ikeda H., Sekiguchi M., Nojima S.;
RT "The DNA sequence encoding pldA gene, the structural gene for detergent-
RT resistant phospholipase A of E. coli.";
RL J. Biochem. 96:1655-1664(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=1379743; DOI=10.1126/science.1379743;
RA Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.;
RT "Analysis of the Escherichia coli genome: DNA sequence of the region from
RT 84.5 to 86.5 minutes.";
RL Science 257:771-778(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO
RP 14-15.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 21-24.
RC STRAIN=K12;
RX PubMed=7556153; DOI=10.1111/j.1432-1033.1995.tb20801.x;
RA Dekker N., Merck K., Tommassen J., Verheij H.M.;
RT "In vitro folding of Escherichia coli outer-membrane phospholipase A.";
RL Eur. J. Biochem. 232:214-219(1995).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 30-289.
RC STRAIN=K12;
RX PubMed=6383820;
RA de Geus P., Verheij H.M., Riegman N.H., Hoekstra W.P.M., de Haas G.H.;
RT "The pro- and mature forms of the E. coli K-12 outer membrane phospholipase
RT A are identical.";
RL EMBO J. 3:1799-1802(1984).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 174-289.
RC STRAIN=K12;
RX PubMed=3027506; DOI=10.1007/bf00430442;
RA Irino N., Nakayama K., Nakayama H.;
RT "The recQ gene of Escherichia coli K12: primary structure and evidence for
RT SOS regulation.";
RL Mol. Gen. Genet. 205:298-304(1986).
RN [8]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12;
RX PubMed=6397463; DOI=10.1093/oxfordjournals.jbchem.a134996;
RA Homma H., Chiba N., Kobayashi T., Kudo I., Inoue K., Ikeda H.,
RA Sekiguchi M., Nojima S.;
RT "Characteristics of detergent-resistant phospholipase A overproduced in E.
RT coli cells bearing its cloned structural gene.";
RL J. Biochem. 96:1645-1653(1984).
RN [9]
RP MUTAGENESIS OF SER-172.
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 [10]
RP ACTIVE SITE SER-164, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2040286; DOI=10.1111/j.1432-1033.1991.tb16008.x;
RA Horrevoets A.J.G., Verheij H.M., de Haas G.H.;
RT "Inactivation of Escherichia coli outer-membrane phospholipase A by the
RT affinity label hexadecanesulfonyl fluoride. Evidence for an active-site
RT serine.";
RL Eur. J. Biochem. 198:247-253(1991).
RN [11]
RP SUBUNIT, AND ACTIVITY REGULATION.
RX PubMed=9013551; DOI=10.1074/jbc.272.6.3179;
RA Dekker N., Tommassen J., Lustig A., Rosenbusch J.P., Verheij H.M.;
RT "Dimerization regulates the enzymatic activity of Escherichia coli outer
RT membrane phospholipase A.";
RL J. Biol. Chem. 272:3179-3184(1997).
RN [12]
RP SUBUNIT, AND ACTIVITY REGULATION.
RX PubMed=10322034; DOI=10.1128/jb.181.10.3281-3283.1999;
RA Dekker N., Tommassen J., Verheij H.M.;
RT "Bacteriocin release protein triggers dimerization of outer membrane
RT phospholipase A in vivo.";
RL J. Bacteriol. 181:3281-3283(1999).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 33-289 IN MONOMERIC AND DIMERIC
RP FORM, COFACTOR, AND SUBUNIT.
RX PubMed=10537112; DOI=10.1038/44890;
RA Snijder H.J., Ubarretxena-Belandia I., Blaauw M., Kalk K.H., Verheij H.M.,
RA Egmond M.R., Dekker N., Dijkstra B.W.;
RT "Structural evidence for dimerization-regulated activation of an integral
RT membrane phospholipase.";
RL Nature 401:717-721(1999).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 21-289 IN MONOMERIC AND DIMERIC
RP FORM IN THE PRESENCE AND ABSENCE OF CALCIUM.
RX PubMed=11371166; DOI=10.1006/jmbi.2001.4675;
RA Snijder H.J., Kingma R.L., Kalk K.H., Dekker N., Egmond M.R.,
RA Dijkstra B.W.;
RT "Structural investigations of calcium binding and its role in activity and
RT activation of outer membrane phospholipase A from Escherichia coli.";
RL J. Mol. Biol. 309:477-489(2001).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 21-289 OF MUTANT ALA-156.
RX PubMed=11567087; DOI=10.1110/ps.17701;
RA Snijder H.J., Van Eerde J.H., Kingma R.L., Kalk K.H., Dekker N.,
RA Egmond M.R., Dijkstra B.W.;
RT "Structural investigations of the active-site mutant Asn156Ala of outer
RT membrane phospholipase A: function of the Asn-His interaction in the
RT catalytic triad.";
RL Protein Sci. 10:1962-1969(2001).
CC -!- FUNCTION: Has broad substrate specificity including hydrolysis of
CC phosphatidylcholine with phospholipase A2 (EC 3.1.1.4) and
CC phospholipase A1 (EC 3.1.1.32) activities. Strong expression leads to
CC outer membrane breakdown and cell death; is dormant in normal growing
CC cells. Required for efficient secretion of bacteriocins.
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;
CC Evidence={ECO:0000269|PubMed:10537112};
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 (Arg-167 and Ser-172 from 1 monomer,
CC Ser-126 of the other). The Ca(2+) ion may have a role in catalysis.
CC {ECO:0000269|PubMed:10537112};
CC -!- ACTIVITY REGULATION: By membrane damage, for example, by phage-induced
CC lysis or temperature shock. The protein is inactive in the monomeric
CC form and active in the dimeric form; calcium is essential for dimer
CC stability. {ECO:0000269|PubMed:10322034, ECO:0000269|PubMed:9013551}.
CC -!- SUBUNIT: Homodimer; dimerization is reversible, and the dimeric form is
CC the active one. {ECO:0000269|PubMed:10322034,
CC ECO:0000269|PubMed:10537112, ECO:0000269|PubMed:9013551}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:6397463};
CC Multi-pass membrane protein {ECO:0000269|PubMed:6397463}. Note=One of
CC the very few enzymes located there.
CC -!- SIMILARITY: Belongs to the phospholipase A1 family. {ECO:0000305}.
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DR EMBL; X02143; CAA26081.1; -; Genomic_DNA.
DR EMBL; M87049; AAA67617.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76824.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77480.1; -; Genomic_DNA.
DR EMBL; M30198; AAA24516.1; -; Genomic_DNA.
DR PIR; A22133; PSECA1.
DR RefSeq; NP_418265.1; NC_000913.3.
DR RefSeq; WP_001259700.1; NZ_SSZK01000046.1.
DR PDB; 1FW2; X-ray; 2.60 A; A=21-289.
DR PDB; 1FW3; X-ray; 2.80 A; A/B=21-289.
DR PDB; 1ILD; X-ray; 2.80 A; A=21-289.
DR PDB; 1ILZ; X-ray; 2.50 A; A=21-289.
DR PDB; 1IM0; X-ray; 2.98 A; A=21-289.
DR PDB; 1QD5; X-ray; 2.17 A; A=21-289.
DR PDB; 1QD6; X-ray; 2.10 A; A/B=33-45, C/D=50-289.
DR PDB; 6LYQ; X-ray; 3.19 A; O=274-289.
DR PDBsum; 1FW2; -.
DR PDBsum; 1FW3; -.
DR PDBsum; 1ILD; -.
DR PDBsum; 1ILZ; -.
DR PDBsum; 1IM0; -.
DR PDBsum; 1QD5; -.
DR PDBsum; 1QD6; -.
DR PDBsum; 6LYQ; -.
DR AlphaFoldDB; P0A921; -.
DR SMR; P0A921; -.
DR BioGRID; 4259303; 274.
DR IntAct; P0A921; 12.
DR STRING; 511145.b3821; -.
DR DrugBank; DB03692; 1-Hexadecanosulfonyl-O-L-Serine.
DR jPOST; P0A921; -.
DR PaxDb; P0A921; -.
DR PRIDE; P0A921; -.
DR EnsemblBacteria; AAC76824; AAC76824; b3821.
DR EnsemblBacteria; BAE77480; BAE77480; BAE77480.
DR GeneID; 66672271; -.
DR GeneID; 948307; -.
DR KEGG; ecj:JW3794; -.
DR KEGG; eco:b3821; -.
DR PATRIC; fig|1411691.4.peg.2886; -.
DR EchoBASE; EB0731; -.
DR eggNOG; COG2829; Bacteria.
DR HOGENOM; CLU_045813_1_0_6; -.
DR InParanoid; P0A921; -.
DR OMA; WGGCRSV; -.
DR PhylomeDB; P0A921; -.
DR BioCyc; EcoCyc:MON0-341; -.
DR BioCyc; MetaCyc:MON0-341; -.
DR EvolutionaryTrace; P0A921; -.
DR PRO; PR:P0A921; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IDA:EcoCyc.
DR GO; GO:0045203; C:integral component of cell outer membrane; IDA:EcoCyc.
DR GO; GO:0031230; C:intrinsic component of cell outer membrane; IDA:UniProtKB.
DR GO; GO:0052740; F:1-acyl-2-lysophosphatidylserine acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0004622; F:lysophospholipase activity; IDA:EcoCyc.
DR GO; GO:0052739; F:phosphatidylserine 1-acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008970; F:phospholipase A1 activity; TAS:UniProtKB.
DR GO; GO:0004623; F:phospholipase A2 activity; IDA:EcoCyc.
DR GO; GO:0004620; F:phospholipase activity; IDA:EcoCyc.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046471; P:phosphatidylglycerol metabolic process; IDA:EcoCyc.
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; Direct protein sequencing;
KW Hydrolase; Lipid degradation; Lipid metabolism; Membrane; Metal-binding;
KW Reference proteome; Signal; Transmembrane; Transmembrane beta strand.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:6397464,
FT ECO:0000269|PubMed:7556153"
FT CHAIN 21..289
FT /note="Phospholipase A1"
FT /id="PRO_0000021983"
FT TOPO_DOM 21..52
FT /note="Periplasmic"
FT TRANSMEM 53..65
FT /note="Beta stranded"
FT TOPO_DOM 66..84
FT /note="Extracellular"
FT TRANSMEM 85..99
FT /note="Beta stranded"
FT TOPO_DOM 100..105
FT /note="Periplasmic"
FT TRANSMEM 106..118
FT /note="Beta stranded"
FT TOPO_DOM 119..128
FT /note="Extracellular"
FT TRANSMEM 129..148
FT /note="Beta stranded"
FT TOPO_DOM 149..150
FT /note="Periplasmic"
FT TRANSMEM 151..164
FT /note="Beta stranded"
FT TOPO_DOM 165..173
FT /note="Extracellular"
FT TRANSMEM 174..186
FT /note="Beta stranded"
FT TOPO_DOM 187..188
FT /note="Periplasmic"
FT TRANSMEM 189..198
FT /note="Beta stranded"
FT TOPO_DOM 199..216
FT /note="Extracellular"
FT TRANSMEM 217..223
FT /note="Beta stranded"
FT TOPO_DOM 224..225
FT /note="Periplasmic"
FT TRANSMEM 226..234
FT /note="Beta stranded"
FT TOPO_DOM 235..241
FT /note="Extracellular"
FT TRANSMEM 242..250
FT /note="Beta stranded"
FT TOPO_DOM 251..255
FT /note="Periplasmic"
FT TRANSMEM 256..265
FT /note="Beta stranded"
FT TOPO_DOM 266..274
FT /note="Extracellular"
FT TRANSMEM 275..286
FT /note="Beta stranded"
FT TOPO_DOM 287..289
FT /note="Periplasmic"
FT ACT_SITE 162
FT /note="Proton acceptor"
FT /evidence="ECO:0000305"
FT ACT_SITE 164
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:2040286"
FT BINDING 126
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /note="in dimeric form"
FT BINDING 167
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /note="in dimeric form"
FT BINDING 172
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /note="in dimeric form"
FT BINDING 204
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /note="in monomeric form"
FT MUTAGEN 172
FT /note="S->F: Inactive protein."
FT /evidence="ECO:0000269|PubMed:8300539"
FT CONFLICT 14..15
FT /note="LP -> FA (in Ref. 2; AAA67617)"
FT /evidence="ECO:0000305"
FT CONFLICT 30..33
FT /note="DAPA -> MTRQ (in Ref. 6)"
FT /evidence="ECO:0000305"
FT HELIX 38..43
FT /evidence="ECO:0007829|PDB:1QD6"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:1QD6"
FT STRAND 59..67
FT /evidence="ECO:0007829|PDB:1QD6"
FT TURN 70..75
FT /evidence="ECO:0007829|PDB:1QD6"
FT HELIX 77..81
FT /evidence="ECO:0007829|PDB:1QD6"
FT STRAND 84..99
FT /evidence="ECO:0007829|PDB:1QD6"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:1QD6"
FT STRAND 106..118
FT /evidence="ECO:0007829|PDB:1QD6"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:1QD6"
FT STRAND 129..148
FT /evidence="ECO:0007829|PDB:1QD6"
FT STRAND 151..164
FT /evidence="ECO:0007829|PDB:1QD6"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:1ILZ"
FT STRAND 174..186
FT /evidence="ECO:0007829|PDB:1QD6"
FT STRAND 189..200
FT /evidence="ECO:0007829|PDB:1QD6"
FT HELIX 208..212
FT /evidence="ECO:0007829|PDB:1QD6"
FT STRAND 214..223
FT /evidence="ECO:0007829|PDB:1QD6"
FT STRAND 226..234
FT /evidence="ECO:0007829|PDB:1QD6"
FT TURN 236..238
FT /evidence="ECO:0007829|PDB:1QD6"
FT STRAND 241..252
FT /evidence="ECO:0007829|PDB:1QD6"
FT STRAND 255..265
FT /evidence="ECO:0007829|PDB:1QD6"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:1QD6"
FT STRAND 275..285
FT /evidence="ECO:0007829|PDB:1QD6"
SQ SEQUENCE 289 AA; 33163 MW; A688AD32AA60F218 CRC64;
MRTLQGWLLP VFMLPMAVYA QEATVKEVHD APAVRGSIIA NMLQEHDNPF TLYPYDTNYL
IYTQTSDLNK EAIASYDWAE NARKDEVKFQ LSLAFPLWRG ILGPNSVLGA SYTQKSWWQL
SNSEESSPFR ETNYEPQLFL GFATDYRFAG WTLRDVEMGY NHDSNGRSDP TSRSWNRLYT
RLMAENGNWL VEVKPWYVVG NTDDNPDITK YMGYYQLKIG YHLGDAVLSA KGQYNWNTGY
GGAELGLSYP ITKHVRLYTQ VYSGYGESLI DYNFNQTRVG VGVMLNDLF
