PLD_RICCN
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 03-AUG-2022, entry version 92.
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; Proteobacteria; 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 EnsemblBacteria; AAL03808; AAL03808; RC1270.
DR KEGG; rco:RC1270; -.
DR HOGENOM; CLU_080814_3_0_5; -.
DR OMA; QRTEKYS; -.
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: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 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
