ID   PLD_RICPR               Reviewed;         205 AA.
AC   Q9ZCD8;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Phospholipase D;
DE            Short=PLD;
DE            EC=3.1.4.4;
DE   AltName: Full=Choline phosphatase;
DE   Flags: Precursor;
GN   Name=pld; OrderedLocusNames=RP819;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
RN   [2]
RP   FUNCTION.
RC   STRAIN=ATCC VR-142 / Breinl;
RX   PubMed=14593584; DOI=10.1086/379080;
RA   Renesto P., Dehoux P., Gouin E., Touqui L., Cossart P., Raoult D.;
RT   "Identification and characterization of a phospholipase D-superfamily gene
RT   in Rickettsiae.";
RL   J. Infect. Dis. 188:1276-1283(2003).
CC   -!- FUNCTION: Could be a virulence factor. {ECO:0000269|PubMed:14593584}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-
CC         sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:14445,
CC         ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57643, ChEBI:CHEBI:58608; EC=3.1.4.4;
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the phospholipase D family. {ECO:0000305}.
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DR   EMBL; AJ235273; CAA15244.1; -; Genomic_DNA.
DR   PIR; D71643; D71643.
DR   RefSeq; NP_221168.1; NC_000963.1.
DR   RefSeq; WP_004596866.1; NC_000963.1.
DR   AlphaFoldDB; Q9ZCD8; -.
DR   SMR; Q9ZCD8; -.
DR   STRING; 272947.RP819; -.
DR   EnsemblBacteria; CAA15244; CAA15244; CAA15244.
DR   GeneID; 57569941; -.
DR   KEGG; rpr:RP819; -.
DR   PATRIC; fig|272947.5.peg.854; -.
DR   eggNOG; COG1502; Bacteria.
DR   HOGENOM; CLU_080814_3_0_5; -.
DR   OMA; RYLTHWQ; -.
DR   Proteomes; UP000002480; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
DR   GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-EC.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0019637; P:organophosphate metabolic process; IEA:UniProt.
DR   InterPro; IPR025202; PLD-like_dom.
DR   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   Pfam; PF13091; PLDc_2; 1.
DR   SMART; SM00155; PLDc; 1.
DR   PROSITE; PS50035; PLD; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Lipid degradation; Lipid metabolism; Reference proteome;
KW   Secreted; Signal; Virulence.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..205
FT                   /note="Phospholipase D"
FT                   /id="PRO_0000274784"
FT   DOMAIN          142..169
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT   ACT_SITE        147
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT   ACT_SITE        149
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT   ACT_SITE        154
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
SQ   SEQUENCE   205 AA;  23078 MW;  D02C9240B8A8CC5A CRC64;
     MKSKNNKFIA VSISFILGIA LGIYVESTYY FTNIINSKSF SLSNAQINYY SISELSRSNV
     STCFTPPAGC TKFIVQQIEK AEESIYMQAY GMSDSLITTA LINAQMRGVK VRILLDRSNL
     KQKFSKLYEL QQAKIDVGID TVPGIAHNKV IIIDKKKVIT GSFNFTVSAD KRNAENVILI
     EDRKLAESYL QNWFSRKTTS NAVHF