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   16-JUN-2009, entry version 23.
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.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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
RT   in gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(2006).
CC   -!- FUNCTION: Could be a virulence factor (By similarity).
CC   -!- CATALYTIC ACTIVITY: A phosphatidylcholine + H(2)O = choline + a
CC       phosphatidate.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted (Potential).
CC   -!- SIMILARITY: Belongs to the phospholipase D family.
CC   -!- SIMILARITY: Contains 1 PLD phosphodiesterase domain.
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DR   EMBL; CP000087; ABE04256.1; -; Genomic_DNA.
DR   RefSeq; YP_537345.1; -.
DR   GeneID; 3995535; -.
DR   GenomeReviews; CP000087_GR; RBE_0175.
DR   KEGG; rbe:RBE_0175; -.
DR   HOGENOM; Q1RK58; -.
DR   OMA; Q1RK58; TVPGIAH.
DR   BioCyc; RBEL336407:RBE_0175-MON; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0070290; F:NAPE-specific phospholipase D activity; IEA:EC.
DR   GO; GO:0004630; F:phospholipase D activity; IEA:EC.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
DR   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   SMART; SM00155; PLDc; 1.
DR   PROSITE; PS50035; PLD; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Hydrolase; Lipid degradation; Secreted; Signal;
KW   Virulence.
FT   SIGNAL        1     25       Potential.
FT   CHAIN        26    201       Phospholipase D.
FT                                /FTId=PRO_0000274782.
FT   DOMAIN      142    169       PLD phosphodiesterase.
FT   ACT_SITE    147    147       Potential.
FT   ACT_SITE    149    149       Potential.
FT   ACT_SITE    154    154       Potential.
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
//