ID   PLD_RICCN               Reviewed;         200 AA.
AC   Q92G53;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, 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=RC1270;
OS   Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=272944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-613 / Malish 7;
RX   PubMed=11557893; DOI=10.1126/science.1061471;
RA   Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA   Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT   "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL   Science 293:2093-2098(2001).
RN   [2]
RP   PROTEIN SEQUENCE OF 58-77, FUNCTION, SUBUNIT, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC VR-613 / Malish 7;
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         Evidence={ECO:0000269|PubMed:14593584};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14593584}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the phospholipase D family. {ECO:0000305}.
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DR   EMBL; AE006914; AAL03808.1; -; Genomic_DNA.
DR   PIR; F97858; F97858.
DR   RefSeq; WP_010977832.1; NC_003103.1.
DR   AlphaFoldDB; Q92G53; -.
DR   SMR; Q92G53; -.
DR   GeneID; 928420; -.
DR   KEGG; rco:RC1270; -.
DR   HOGENOM; CLU_080814_3_0_5; -.
DR   Proteomes; UP000000816; 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:0006793; P:phosphorus metabolic process; IEA:UniProt.
DR   CDD; cd09170; PLDc_Nuc; 1.
DR   Gene3D; 3.30.870.10; Endonuclease Chain A; 1.
DR   InterPro; IPR025202; PLD-like_dom.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Secreted; Signal; Virulence.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..200
FT                   /note="Phospholipase D"
FT                   /id="PRO_0000274781"
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;  22418 MW;  F878E8D78AF6E6F5 CRC64;
     MKRKNNKFIE ISIAFILGIA LGLYGQNPDY FTNLISQKSL ALSALQIKHY NISELSRSKV
     STCFTPPAGC TKFIANQIDK AEESIYMQAY GMSDALITTA LINAQARGVK VRILLDRSNL
     KQKFSKLHEL QRAKIDVDID KVPGIAHNKV IIIDKKKVIT GSFNFTAAAD KRNAENVIII
     EDQELAESYL QNWLNRKASN
//