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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) (OMPLA) (Phosphatidylcholine 1-acylhydrolase)

 PA1_ECOLI               Reviewed;         289 AA.
P0A921; P00631; Q2M8C6;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
19-JUL-2005, sequence version 1.
05-DEC-2018, entry version 103.
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;
Short=OMPLA;
AltName: Full=Phosphatidylcholine 1-acylhydrolase;
Flags: Precursor;
Name=pldA; OrderedLocusNames=b3821, JW3794;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 21-30.
STRAIN=K12;
PubMed=6397464;
Homma H., Kobayashi T., Chiba N., Karasawa K., Mizushima H., Kudo I.,
Inoue K., Ikeda H., Sekiguchi M., Nojima S.;
"The DNA sequence encoding pldA gene, the structural gene for
detergent-resistant phospholipase A of E. coli.";
J. Biochem. 96:1655-1664(1984).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=1379743; DOI=10.1126/science.1379743;
Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.;
"Analysis of the Escherichia coli genome: DNA sequence of the region
from 84.5 to 86.5 minutes.";
Science 257:771-778(1992).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION
TO 14-15.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
PROTEIN SEQUENCE OF 21-24.
STRAIN=K12;
PubMed=7556153; DOI=10.1111/j.1432-1033.1995.tb20801.x;
Dekker N., Merck K., Tommassen J., Verheij H.M.;
"In vitro folding of Escherichia coli outer-membrane phospholipase
A.";
Eur. J. Biochem. 232:214-219(1995).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 30-289.
STRAIN=K12;
PubMed=6383820;
de Geus P., Verheij H.M., Riegman N.H., Hoekstra W.P.M., de Haas G.H.;
"The pro- and mature forms of the E. coli K-12 outer membrane
phospholipase A are identical.";
EMBO J. 3:1799-1802(1984).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 174-289.
STRAIN=K12;
PubMed=3027506; DOI=10.1007/BF00430442;
Irino N., Nakayama K., Nakayama H.;
"The recQ gene of Escherichia coli K12: primary structure and evidence
for SOS regulation.";
Mol. Gen. Genet. 205:298-304(1986).
[8]
SUBCELLULAR LOCATION.
STRAIN=K12;
PubMed=6397463;
Homma H., Chiba N., Kobayashi T., Kudo I., Inoue K., Ikeda H.,
Sekiguchi M., Nojima S.;
"Characteristics of detergent-resistant phospholipase A overproduced
in E. coli cells bearing its cloned structural gene.";
J. Biochem. 96:1645-1653(1984).
[9]
MUTAGENESIS OF SER-172.
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).
[10]
ACTIVE SITE SER-164, AND PARTIAL PROTEIN SEQUENCE.
PubMed=2040286; DOI=10.1111/j.1432-1033.1991.tb16008.x;
Horrevoets A.J.G., Verheij H.M., de Haas G.H.;
"Inactivation of Escherichia coli outer-membrane phospholipase A by
the affinity label hexadecanesulfonyl fluoride. Evidence for an
active-site serine.";
Eur. J. Biochem. 198:247-253(1991).
[11]
SUBUNIT, AND ACTIVITY REGULATION.
PubMed=9013551; DOI=10.1074/jbc.272.6.3179;
Dekker N., Tommassen J., Lustig A., Rosenbusch J.P., Verheij H.M.;
"Dimerization regulates the enzymatic activity of Escherichia coli
outer membrane phospholipase A.";
J. Biol. Chem. 272:3179-3184(1997).
[12]
SUBUNIT, AND ACTIVITY REGULATION.
PubMed=10322034;
Dekker N., Tommassen J., Verheij H.M.;
"Bacteriocin release protein triggers dimerization of outer membrane
phospholipase A in vivo.";
J. Bacteriol. 181:3281-3283(1999).
[13]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 33-289 IN MONOMERIC AND
DIMERIC FORM, COFACTOR, AND SUBUNIT.
PubMed=10537112; DOI=10.1038/401717a0;
Snijder H.J., Ubarretxena-Belandia I., Blaauw M., Kalk K.H.,
Verheij H.M., Egmond M.R., Dekker N., Dijkstra B.W.;
"Structural evidence for dimerization-regulated activation of an
integral membrane phospholipase.";
Nature 401:717-721(1999).
[14]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 21-289 IN MONOMERIC AND
DIMERIC FORM IN THE PRESENCE AND ABSENCE OF CALCIUM.
PubMed=11371166; DOI=10.1006/jmbi.2001.4675;
Snijder H.J., Kingma R.L., Kalk K.H., Dekker N., Egmond M.R.,
Dijkstra B.W.;
"Structural investigations of calcium binding and its role in activity
and activation of outer membrane phospholipase A from Escherichia
coli.";
J. Mol. Biol. 309:477-489(2001).
[15]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 21-289 OF MUTANT ALA-156.
PubMed=11567087; DOI=10.1110/ps.17701;
Snijder H.J., Van Eerde J.H., Kingma R.L., Kalk K.H., Dekker N.,
Egmond M.R., Dijkstra B.W.;
"Structural investigations of the active-site mutant Asn156Ala of
outer membrane phospholipase A: function of the Asn-His interaction in
the catalytic triad.";
Protein Sci. 10:1962-1969(2001).
-!- FUNCTION: Has broad substrate specificity including hydrolysis of
phosphatidylcholine with phospholipase A2 (EC 3.1.1.4) and
phospholipase A1 (EC 3.1.1.32) activities. Strong expression leads
to outer membrane breakdown and cell death; is dormant in normal
growing cells. Required for efficient secretion of bacteriocins.
-!- 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:0000269|PubMed:10537112};
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 (Arg-167 and
Ser-172 from 1 monomer, Ser-126 of the other). The Ca(2+) ion may
have a role in catalysis. {ECO:0000269|PubMed:10537112};
-!- ACTIVITY REGULATION: By membrane damage, for example, by phage-
induced lysis or temperature shock. The protein is inactive in the
monomeric form and active in the dimeric form; calcium is
essential for dimer stability. {ECO:0000269|PubMed:10322034,
ECO:0000269|PubMed:9013551}.
-!- SUBUNIT: Homodimer; dimerization is reversible, and the dimeric
form is the active one. {ECO:0000269|PubMed:10322034,
ECO:0000269|PubMed:10537112, ECO:0000269|PubMed:9013551}.
-!- SUBCELLULAR LOCATION: Cell outer membrane
{ECO:0000269|PubMed:6397463}; Multi-pass membrane protein
{ECO:0000269|PubMed:6397463}. Note=One of the very few enzymes
located there.
-!- SIMILARITY: Belongs to the phospholipase A1 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X02143; CAA26081.1; -; Genomic_DNA.
EMBL; M87049; AAA67617.1; -; Genomic_DNA.
EMBL; U00096; AAC76824.1; -; Genomic_DNA.
EMBL; AP009048; BAE77480.1; -; Genomic_DNA.
EMBL; M30198; AAA24516.1; -; Genomic_DNA.
PIR; A22133; PSECA1.
RefSeq; NP_418265.1; NC_000913.3.
RefSeq; WP_001259700.1; NZ_LN832404.1.
PDB; 1FW2; X-ray; 2.60 A; A=21-289.
PDB; 1FW3; X-ray; 2.80 A; A/B=21-289.
PDB; 1ILD; X-ray; 2.80 A; A=21-289.
PDB; 1ILZ; X-ray; 2.50 A; A=21-289.
PDB; 1IM0; X-ray; 2.98 A; A=21-289.
PDB; 1QD5; X-ray; 2.17 A; A=21-289.
PDB; 1QD6; X-ray; 2.10 A; A/B=33-45, C/D=50-289.
PDBsum; 1FW2; -.
PDBsum; 1FW3; -.
PDBsum; 1ILD; -.
PDBsum; 1ILZ; -.
PDBsum; 1IM0; -.
PDBsum; 1QD5; -.
PDBsum; 1QD6; -.
ProteinModelPortal; P0A921; -.
SMR; P0A921; -.
BioGrid; 4259303; 274.
IntAct; P0A921; 12.
STRING; 316385.ECDH10B_4012; -.
DrugBank; DB03692; 1-Hexadecanosulfonyl-O-L-Serine.
PaxDb; P0A921; -.
PRIDE; P0A921; -.
EnsemblBacteria; AAC76824; AAC76824; b3821.
EnsemblBacteria; BAE77480; BAE77480; BAE77480.
GeneID; 948307; -.
KEGG; ecj:JW3794; -.
KEGG; eco:b3821; -.
PATRIC; fig|1411691.4.peg.2886; -.
EchoBASE; EB0731; -.
EcoGene; EG10738; pldA.
eggNOG; ENOG4105HDD; Bacteria.
eggNOG; COG2829; LUCA.
HOGENOM; HOG000288150; -.
InParanoid; P0A921; -.
KO; K01058; -.
PhylomeDB; P0A921; -.
BioCyc; EcoCyc:MONOMER0-341; -.
BioCyc; MetaCyc:MONOMER0-341; -.
EvolutionaryTrace; P0A921; -.
PRO; PR:P0A921; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0009279; C:cell outer membrane; IDA:EcoCyc.
GO; GO:0045203; C:integral component of cell outer membrane; IDA:EcoCyc.
GO; GO:0031230; C:intrinsic component of cell outer membrane; IDA:UniProtKB.
GO; GO:0052740; F:1-acyl-2-lysophosphatidylserine acylhydrolase activity; IEA:UniProtKB-EC.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0052739; F:phosphatidylserine 1-acylhydrolase activity; IEA:UniProtKB-EC.
GO; GO:0008970; F:phospholipase A1 activity; TAS:UniProtKB.
GO; GO:0004623; F:phospholipase A2 activity; IDA:EcoCyc.
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:0042803; F:protein homodimerization activity; IDA:UniProtKB.
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.
1: Evidence at protein level;
3D-structure; Calcium; Cell outer membrane; Complete proteome;
Direct protein sequencing; Hydrolase; Lipid degradation;
Lipid metabolism; Membrane; Metal-binding; Reference proteome; Signal;
Transmembrane; Transmembrane beta strand.
SIGNAL 1 20 {ECO:0000269|PubMed:6397464,
ECO:0000269|PubMed:7556153}.
CHAIN 21 289 Phospholipase A1.
/FTId=PRO_0000021983.
TOPO_DOM 21 52 Periplasmic.
TRANSMEM 53 65 Beta stranded.
TOPO_DOM 66 84 Extracellular.
TRANSMEM 85 99 Beta stranded.
TOPO_DOM 100 105 Periplasmic.
TRANSMEM 106 118 Beta stranded.
TOPO_DOM 119 128 Extracellular.
TRANSMEM 129 148 Beta stranded.
TOPO_DOM 149 150 Periplasmic.
TRANSMEM 151 164 Beta stranded.
TOPO_DOM 165 173 Extracellular.
TRANSMEM 174 186 Beta stranded.
TOPO_DOM 187 188 Periplasmic.
TRANSMEM 189 198 Beta stranded.
TOPO_DOM 199 216 Extracellular.
TRANSMEM 217 223 Beta stranded.
TOPO_DOM 224 225 Periplasmic.
TRANSMEM 226 234 Beta stranded.
TOPO_DOM 235 241 Extracellular.
TRANSMEM 242 250 Beta stranded.
TOPO_DOM 251 255 Periplasmic.
TRANSMEM 256 265 Beta stranded.
TOPO_DOM 266 274 Extracellular.
TRANSMEM 275 286 Beta stranded.
TOPO_DOM 287 289 Periplasmic.
ACT_SITE 162 162 Proton acceptor. {ECO:0000305}.
ACT_SITE 164 164 Nucleophile.
{ECO:0000269|PubMed:2040286}.
METAL 126 126 Calcium 1; via carbonyl oxygen; in
dimeric form.
METAL 167 167 Calcium 2; via carbonyl oxygen; in
dimeric form.
METAL 172 172 Calcium 2; in dimeric form.
METAL 204 204 Calcium 3; in monomeric form.
MUTAGEN 172 172 S->F: Inactive protein.
{ECO:0000269|PubMed:8300539}.
CONFLICT 14 15 LP -> FA (in Ref. 2; AAA67617).
{ECO:0000305}.
CONFLICT 30 33 DAPA -> MTRQ (in Ref. 6). {ECO:0000305}.
HELIX 38 43 {ECO:0000244|PDB:1QD6}.
STRAND 52 54 {ECO:0000244|PDB:1QD6}.
STRAND 59 67 {ECO:0000244|PDB:1QD6}.
TURN 70 75 {ECO:0000244|PDB:1QD6}.
HELIX 77 81 {ECO:0000244|PDB:1QD6}.
STRAND 84 99 {ECO:0000244|PDB:1QD6}.
TURN 100 102 {ECO:0000244|PDB:1QD6}.
STRAND 106 118 {ECO:0000244|PDB:1QD6}.
HELIX 123 125 {ECO:0000244|PDB:1QD6}.
STRAND 129 148 {ECO:0000244|PDB:1QD6}.
STRAND 151 164 {ECO:0000244|PDB:1QD6}.
STRAND 169 171 {ECO:0000244|PDB:1ILZ}.
STRAND 174 186 {ECO:0000244|PDB:1QD6}.
STRAND 189 200 {ECO:0000244|PDB:1QD6}.
HELIX 208 212 {ECO:0000244|PDB:1QD6}.
STRAND 214 223 {ECO:0000244|PDB:1QD6}.
STRAND 226 234 {ECO:0000244|PDB:1QD6}.
TURN 236 238 {ECO:0000244|PDB:1QD6}.
STRAND 241 252 {ECO:0000244|PDB:1QD6}.
STRAND 255 265 {ECO:0000244|PDB:1QD6}.
HELIX 269 271 {ECO:0000244|PDB:1QD6}.
STRAND 275 285 {ECO:0000244|PDB:1QD6}.
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


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