ID   PLD_RICBR               Reviewed;         201 AA.
AC   Q1RK58;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 85.
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; Synonyms=pldA; OrderedLocusNames=RBE_0175;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RML369-C;
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT   gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(2006).
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; CP000087; ABE04256.1; -; Genomic_DNA.
DR   RefSeq; WP_011476870.1; NC_007940.1.
DR   AlphaFoldDB; Q1RK58; -.
DR   SMR; Q1RK58; -.
DR   STRING; 336407.RBE_0175; -.
DR   EnsemblBacteria; ABE04256; ABE04256; RBE_0175.
DR   KEGG; rbe:RBE_0175; -.
DR   eggNOG; COG1502; Bacteria.
DR   HOGENOM; CLU_080814_3_0_5; -.
DR   OMA; RYLTHWQ; -.
DR   OrthoDB; 1992731at2; -.
DR   Proteomes; UP000001951; 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..201
FT                   /note="Phospholipase D"
FT                   /id="PRO_0000274782"
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   201 AA;  22440 MW;  79ADA07A9A7B5C78 CRC64;
     MKRKNKKFTE IFIAFILGIA IGVLGYSDYG TDLINQFKIS HTPPPKIKHY NISQLSRSKV
     STCFTPPSGC TKFIADQIDT ARESIYMHAY GMSDSLITAA LIDAQARGVQ VKILLDRSNL
     KQKFSKLHEL QRAKIEVGID KVPGIAHNKV IIIDKKKVIT GSFNFTAAAD KRNAENVIVI
     EDAELADSYL QNWLSRKARN G