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 24-JAN-2024, entry version 129. 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; Pseudomonadota; 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; DOI=10.1002/j.1460-2075.1984.tb02048.x; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 511145-b3821; -. DR EnsemblBacteria; AAC76824; AAC76824; b3821. DR GeneID; 75204815; -. 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; DVRWGGC; -. DR OrthoDB; 188433at2; -. DR PhylomeDB; P0A921; -. DR BioCyc; EcoCyc:MONOMER0-341; -. DR BioCyc; MetaCyc:MONOMER0-341; -. DR EvolutionaryTrace; P0A921; -. DR PRO; PR:P0A921; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IDA: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; Phospholipase A1; 1. DR InterPro; IPR003187; PLipase_A1. DR InterPro; IPR036541; PLipase_A1_sf. DR PANTHER; PTHR40457; PHOSPHOLIPASE A1; 1. DR PANTHER; PTHR40457:SF1; PHOSPHOLIPASE A1; 1. DR Pfam; PF02253; PLA1; 1. DR PRINTS; PR01486; PHPHLIPASEA1. DR SUPFAM; SSF56931; Outer membrane phospholipase A (OMPLA); 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 //