ID   PLD_RICFE               Reviewed;         200 AA.
AC   Q4UJZ1;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=RF_1297;
OS   Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=315456;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-1525 / URRWXCal2;
RX   PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA   Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA   Parinello H., Claverie J.-M., Raoult D.;
RT   "The genome sequence of Rickettsia felis identifies the first putative
RT   conjugative plasmid in an obligate intracellular parasite.";
RL   PLoS Biol. 3:1-12(2005).
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; CP000053; AAY62148.1; -; Genomic_DNA.
DR   RefSeq; WP_011271597.1; NC_007109.1.
DR   AlphaFoldDB; Q4UJZ1; -.
DR   SMR; Q4UJZ1; -.
DR   STRING; 315456.RF_1297; -.
DR   EnsemblBacteria; AAY62148; AAY62148; RF_1297.
DR   KEGG; rfe:RF_1297; -.
DR   eggNOG; COG1502; Bacteria.
DR   HOGENOM; CLU_080814_3_0_5; -.
DR   OMA; RYLTHWQ; -.
DR   OrthoDB; 1992731at2; -.
DR   Proteomes; UP000008548; 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; Secreted; Signal;
KW   Virulence.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..200
FT                   /note="Phospholipase D"
FT                   /id="PRO_0000274783"
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   200 AA;  22501 MW;  23E3ABF9A152C41B CRC64;
     MKRKNNKFIE ISIAFILGVA LGIYGQNPDY FTNLINQKSL ASSAPKIKHY NISELLRSKV
     STCFTPPAGC TKFIANQIDR AEESIYMQAY GMSDALITTA LINAQMRGVK VRILLDRSNL
     KQKFSKLHEL QRAKIDVGID KVPGIAHNKV IIIDRKKVIT GSFNFTAAAD KRNAENVIII
     EDRELAESYL QNWLNRKASN