ID   PLD_RICTY               Reviewed;         204 AA.
AC   Q68VT0;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   02-SEP-2026, entry version 97.
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=RT0807;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Rickettsiales; Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
CC   -!- FUNCTION: Could be a virulence factor. {ECO:0000250}.
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; AE017197; AAU04262.1; -; Genomic_DNA.
DR   RefSeq; WP_011191236.1; NC_006142.1.
DR   AlphaFoldDB; Q68VT0; -.
DR   SMR; Q68VT0; -.
DR   KEGG; rty:RT0807; -.
DR   eggNOG; COG1502; Bacteria.
DR   HOGENOM; CLU_080814_3_0_5; -.
DR   OrthoDB; 9762009at2; -.
DR   Proteomes; UP000000604; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004630; F:D-type glycerophospholipase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016891; F:RNA endonuclease activity producing 5'-phosphomonoesters, hydrolytic mechanism; IEA:TreeGrafter.
DR   GO; GO:0006793; P:phosphorus metabolic process; IEA:UniProtKB-ARBA.
DR   CDD; cd09170; PLDc_Nuc; 1.
DR   Gene3D; 3.30.870.10; Endonuclease Chain A; 1.
DR   InterPro; IPR025202; PLD-like_dom.
DR   InterPro; IPR051406; PLD_domain.
DR   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   PANTHER; PTHR43856; CARDIOLIPIN HYDROLASE; 1.
DR   PANTHER; PTHR43856:SF1; MITOCHONDRIAL CARDIOLIPIN HYDROLASE; 1.
DR   Pfam; PF13091; PLDc_2; 1.
DR   SMART; SM00155; PLDc; 1.
DR   SUPFAM; SSF56024; Phospholipase D/nuclease; 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..204
FT                   /note="Phospholipase D"
FT                   /id="PRO_0000274785"
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   204 AA;  23027 MW;  028CDDBACBB5ACEA CRC64;
     MKSKNNKFIA MSIPFILGTA LGIYVESTYY FTSIINQKSF ALPDTQIKHY SIPELSRRNV
     STCFTPPAGC TKFIVQQLEK AEESIYMQAY GMSDSLITTA LINAQMRGVK VKILLDRSNL
     KQKFSKLYEL QQAKIDVGID TVPGIAHNKV IIIDKKKVIT GSFNFTVAAD KRNAENVILI
     EDQQLAESYL QNWFSRKASN SVHF
//