PLD_CORPS
ID PLD_CORPS Reviewed; 307 AA.
AC P20626; Q59314;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Phospholipase D {ECO:0000303|PubMed:2403529, ECO:0000303|PubMed:2407718};
DE Short=PLD {ECO:0000303|PubMed:2403529, ECO:0000303|PubMed:2407718};
DE EC=3.1.4.- {ECO:0000269|PubMed:14732720};
DE AltName: Full=Choline phosphatase;
DE AltName: Full=SM/LPC-specific PLD {ECO:0000303|PubMed:14732720};
DE AltName: Full=Sphingomyelinase D {ECO:0000303|PubMed:14732720};
DE Short=SMaseD {ECO:0000303|PubMed:14732720};
DE EC=3.1.4.41 {ECO:0000269|PubMed:14732720, ECO:0000269|PubMed:2403529};
DE Flags: Precursor;
GN Name=pld;
OS Corynebacterium pseudotuberculosis.
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=1719;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 25-47.
RX PubMed=2407718; DOI=10.1128/jb.172.3.1256-1261.1990;
RA Hodgson A.L.M., Bird P., Nisbet I.T.;
RT "Cloning, nucleotide sequence, and expression in Escherichia coli of the
RT phospholipase D gene from Corynebacterium pseudotuberculosis.";
RL J. Bacteriol. 172:1256-1261(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=Biovar ovis / Isolate Whetten 1;
RX PubMed=2403529; DOI=10.1128/iai.58.1.131-136.1990;
RA Songer J.G., Libby S.J., Iandolo J.J., Cuevas W.A.;
RT "Cloning and expression of the phospholipase D gene from Corynebacterium
RT pseudotuberculosis in Escherichia coli.";
RL Infect. Immun. 58:131-136(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Biovar equi / Isolate 155;
RX PubMed=7737503; DOI=10.1016/0378-1119(95)00002-n;
RA McNamara P.J., Cuevas W.A., Songer J.G.;
RT "Toxic phospholipases D of Corynebacterium pseudotuberculosis, C. ulcerans
RT and Arcanobacterium haemolyticum: cloning and sequence homology.";
RL Gene 156:113-118(1995).
RN [4]
RP MUTAGENESIS.
RC STRAIN=Biovar ovis / Isolate Whetten 1;
RX PubMed=7934899; DOI=10.1111/j.1365-2958.1994.tb01080.x;
RA McNamara P.J., Bradley G.A., Songer J.G.;
RT "Targeted mutagenesis of the phospholipase D gene results in decreased
RT virulence of Corynebacterium pseudotuberculosis.";
RL Mol. Microbiol. 12:921-930(1994).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBSTRATE SPECIFICITY.
RX PubMed=14732720; DOI=10.1074/jbc.c300563200;
RA van Meeteren L.A., Frederiks F., Giepmans B.N., Pedrosa M.F.,
RA Billington S.J., Jost B.H., Tambourgi D.V., Moolenaar W.H.;
RT "Spider and bacterial sphingomyelinases D target cellular lysophosphatidic
RT acid receptors by hydrolyzing lysophosphatidylcholine.";
RL J. Biol. Chem. 279:10833-10836(2004).
CC -!- FUNCTION: Virulence factor affecting bacterial dissemination and
CC survival within the host (PubMed:2403529). Has magnesium-dependent
CC catalytic activity toward sphingomyelin (SM) and acyl- and alkyl-
CC lysophosphatidylcholine (LPC), but not toward
CC sphingosylphosphorylcholine (SPC) and phosphatidylcholine (PC)
CC (PubMed:2403529, PubMed:14732720). Lysophosphatidic acid (LPA), assumed
CC to result from LPC hydrolysis, evokes pathophysiological responses
CC after LPA receptor internalization (PubMed:14732720). Shows hemolytic
CC activity (PubMed:2403529). {ECO:0000269|PubMed:14732720,
CC ECO:0000269|PubMed:2403529}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a sphingomyelin + H2O = an N-acylsphing-4-enine 1-phosphate +
CC choline + H(+); Xref=Rhea:RHEA:20984, ChEBI:CHEBI:15354,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17636,
CC ChEBI:CHEBI:57674; EC=3.1.4.41;
CC Evidence={ECO:0000269|PubMed:14732720, ECO:0000269|PubMed:2403529};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = 1-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphate + choline + H(+);
CC Xref=Rhea:RHEA:38915, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28610, ChEBI:CHEBI:74544;
CC Evidence={ECO:0000269|PubMed:14732720};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-sn-glycero-3-phosphocholine + H2O = 1-O-
CC hexadecyl-sn-glycero-3-phosphate + choline + H(+);
CC Xref=Rhea:RHEA:41143, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:64496, ChEBI:CHEBI:77580;
CC Evidence={ECO:0000269|PubMed:14732720};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:14732720};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=21.8 uM for 1-oleoyl-LPC {ECO:0000269|PubMed:14732720};
CC Vmax=66 nmol/min/mg enzyme toward 1-oleoyl-LPC
CC {ECO:0000269|PubMed:14732720};
CC -!- SIMILARITY: Belongs to the sphingomyelinase D/phospholipase D family.
CC {ECO:0000305}.
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DR EMBL; L16587; AAA64910.1; -; Genomic_DNA.
DR EMBL; L16586; AAA99867.1; -; Genomic_DNA.
DR PIR; A35125; A35125.
DR RefSeq; WP_013240889.1; NZ_RBXH01000001.1.
DR RefSeq; WP_014366232.1; NZ_CP046734.1.
DR AlphaFoldDB; P20626; -.
DR SMR; P20626; -.
DR PRIDE; P20626; -.
DR GeneID; 12297752; -.
DR PATRIC; fig|1719.1052.peg.28; -.
DR OMA; WLDLKNP; -.
DR OrthoDB; 697975at2; -.
DR SABIO-RK; P20626; -.
DR GO; GO:0042597; C:periplasmic space; IDA:UniProtKB.
DR GO; GO:0050290; F:sphingomyelin phosphodiesterase D activity; IDA:UniProtKB.
DR GO; GO:0051701; P:biological process involved in interaction with host; IMP:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006684; P:sphingomyelin metabolic process; IDA:UniProtKB.
DR Gene3D; 3.20.20.190; -; 1.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR016674; SMase_D/PLipase_D.
DR PIRSF; PIRSF016632; Phospholipase_actinobac/fun; 1.
DR SUPFAM; SSF51695; SSF51695; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Lipid degradation; Lipid metabolism;
KW Magnesium; Signal; Virulence.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:2407718"
FT CHAIN 25..307
FT /note="Phospholipase D"
FT /evidence="ECO:0000305|PubMed:2407718"
FT /id="PRO_0000022066"
FT ACT_SITE 44
FT /evidence="ECO:0000255"
FT VARIANT 5..6
FT /note="VV -> FA (in strain: Biovar equi /isolate 155)"
FT VARIANT 8
FT /note="F -> L (in strain: Biovar equi / isolate 155)"
FT VARIANT 189
FT /note="E -> G (in strain: Biovar equi / isolate 155)"
FT VARIANT 205
FT /note="N -> D (in strain: Biovar equi / isolate 155)"
FT VARIANT 270
FT /note="I -> M (in strain: Biovar equi / isolate 155)"
FT VARIANT 277
FT /note="A -> P (in strain: Biovar equi / isolate 155)"
SQ SEQUENCE 307 AA; 33884 MW; D3B1334E6FC99875 CRC64;
MREKVVLFLS IIMAIMLPVG NAAAAPVVHN PASTANRPVY AIAHRVLTTQ GVDDAVAIGA
NALEIDFTAW GRGWWADHDG IPTSAGATAE EIFKHIADKR KQGANITFTW LDIKNPDYCR
DARSVCSINA LRDLARKYLE PAGVRVLYGF YKTVGGPAWK TITADLRDGE AVALSGPAQD
VLNDFARSEN KILTKQKIAD YGYYNINQGF GNCYGTWNRT CDQLRKSSEA RDQGKLGKTF
GWTIATGQDA RVNDLLGKAN VDGLIFGFKI THFYRHADTE NSFKAIKRWV DKHSATHHLA
TVADNPW
