ID A0A0Q5QVT0_9SPHN Unreviewed; 482 AA.
AC A0A0Q5QVT0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Phospholipase D {ECO:0000256|ARBA:ARBA00018392};
DE AltName: Full=Choline phosphatase {ECO:0000256|ARBA:ARBA00029594};
GN ORFNames=ASG11_13590 {ECO:0000313|EMBL:KQS01856.1};
OS Sphingomonas sp. Leaf357.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736350 {ECO:0000313|EMBL:KQS01856.1, ECO:0000313|Proteomes:UP000051080};
RN [1] {ECO:0000313|EMBL:KQS01856.1, ECO:0000313|Proteomes:UP000051080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf357 {ECO:0000313|EMBL:KQS01856.1,
RC ECO:0000313|Proteomes:UP000051080};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQS01856.1, ECO:0000313|Proteomes:UP000051080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf357 {ECO:0000313|EMBL:KQS01856.1,
RC ECO:0000313|Proteomes:UP000051080};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Could be a virulence factor. {ECO:0000256|ARBA:ARBA00003145}.
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:0000256|ARBA:ARBA00000798};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQS01856.1}.
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DR EMBL; LMPM01000002; KQS01856.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q5QVT0; -.
DR STRING; 1736350.ASG11_13590; -.
DR OrthoDB; 8828485at2; -.
DR Proteomes; UP000051080; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006793; P:phosphorus metabolic process; IEA:UniProt.
DR CDD; cd09140; PLDc_vPLD1_2_like_bac_1; 1.
DR CDD; cd09143; PLDc_vPLD1_2_like_bac_2; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR InterPro; IPR015679; PLipase_D_fam.
DR PANTHER; PTHR18896:SF76; PHOSPHOLIPASE; 1.
DR PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR Pfam; PF00614; PLDc; 1.
DR Pfam; PF13091; PLDc_2; 1.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR PROSITE; PS50035; PLD; 2.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000051080};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 127..154
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 342..369
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 482 AA; 54066 MW; 947121DF48041E95 CRC64;
MSALEPGRNC WRIETATRAT VIIDADRYFK AARAAMLKAK HQILLIGWDF DARIDLTPDG
DPGDGAPRNV GDFIYWLVKH RPELQVYTLR WDVGALKTLV RGSTIFTVAK WMTHERIHTK
LDGYHPVGGS HHQKIVVIDD CLAFAGGIDM TSERWDTREH LDDQPCRTEP GGRDRYKPWH
DATTALSGPV ASALGHLCRD RWELAGGKPI DPPPATTDCW PDGLDVDFSD IDVAVSRTEP
EMPDHQPVIE IEQLYLDLIA RARRHIYAES QYFASRKIAE AIALRLDEPD GPEIVIINPT
TAQGWLEPIA MDTARARLFQ ALKHHDTHDR LRIYHPVTKG GLPIYVHAKI LVIDDRVLRV
GSSNFNNRSM RLDTECDVTI DADHGADPAC IAAIRDGLIA EHLGSKASRV AAVLVETGSL
IATIDRLRAP GRTLVDYEVP ELSDVEEWLA DNEVLDPEGP GEMFESLSKR GLFRRMQFWR
KG
//
