PLD_RICTY
ID PLD_RICTY Reviewed; 204 AA.
AC Q68VT0;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=RT0807;
OS Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=257363;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-144 / Wilmington;
RX PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA Yu X.-J., Walker D.H., Weinstock G.M.;
RT "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT of other Rickettsiae.";
RL J. Bacteriol. 186:5842-5855(2004).
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; AE017197; AAU04262.1; -; Genomic_DNA.
DR RefSeq; WP_011191236.1; NC_006142.1.
DR AlphaFoldDB; Q68VT0; -.
DR SMR; Q68VT0; -.
DR STRING; 257363.RT0807; -.
DR EnsemblBacteria; AAU04262; AAU04262; RT0807.
DR KEGG; rty:RT0807; -.
DR eggNOG; COG1502; Bacteria.
DR HOGENOM; CLU_080814_3_0_5; -.
DR OMA; RYLTHWQ; -.
DR OrthoDB; 1992731at2; -.
DR Proteomes; UP000000604; 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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..204
FT /note="Phospholipase D"
FT /id="PRO_0000274785"
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 204 AA; 23027 MW; 028CDDBACBB5ACEA CRC64;
MKSKNNKFIA MSIPFILGTA LGIYVESTYY FTSIINQKSF ALPDTQIKHY SIPELSRRNV
STCFTPPAGC TKFIVQQLEK AEESIYMQAY GMSDSLITTA LINAQMRGVK VKILLDRSNL
KQKFSKLYEL QQAKIDVGID TVPGIAHNKV IIIDKKKVIT GSFNFTVAAD KRNAENVILI
EDQQLAESYL QNWFSRKASN SVHF
