ID A0A0Q4LEI9_9SPHN Unreviewed; 475 AA.
AC A0A0Q4LEI9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Phospholipase D {ECO:0000256|ARBA:ARBA00018392};
DE AltName: Full=Choline phosphatase {ECO:0000256|ARBA:ARBA00029594};
GN ORFNames=ASF00_01190 {ECO:0000313|EMBL:KQN31451.1};
OS Sphingomonas sp. Leaf34.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736216 {ECO:0000313|EMBL:KQN31451.1, ECO:0000313|Proteomes:UP000051932};
RN [1] {ECO:0000313|EMBL:KQN31451.1, ECO:0000313|Proteomes:UP000051932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf34 {ECO:0000313|EMBL:KQN31451.1,
RC ECO:0000313|Proteomes:UP000051932};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN31451.1, ECO:0000313|Proteomes:UP000051932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf34 {ECO:0000313|EMBL:KQN31451.1,
RC ECO:0000313|Proteomes:UP000051932};
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:KQN31451.1}.
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DR EMBL; LMLC01000001; KQN31451.1; -; Genomic_DNA.
DR RefSeq; WP_055872992.1; NZ_LMLC01000001.1.
DR AlphaFoldDB; A0A0Q4LEI9; -.
DR OrthoDB; 8828485at2; -.
DR Proteomes; UP000051932; 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 Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 123..150
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 342..364
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 150..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 475 AA; 53712 MW; 3F9E999FF983BFAB CRC64;
MQVGTECWRV ERAEQMAVIV DAEKYFRTAR VAMMAAKRRI LLIGWDFDAR IELEPGVDRP
GEPKKLGDFM LWLVEREPEL EVFVLRWDTG AIKSLFRGST IFTMLKWMKH KRIHTKLDGH
HPTAASHHQK IVIIDDALAF CGGIDMTGDR WDTRDHRDDE PHRVQPSGKP YKPWHDAISA
VQGPIAHALG ELFRRRWHLA GGMKMAAGKP GGTLWPEGLE VDFHDVDVAI ARSEPEMSDQ
VPVYESEALF LGQIARAKRH LYIESQYFAS RKIAEAVAKR LGEANGPEIV IINPTTAQGW
LEPIAMDTAR ARLMEALHRR DTYGRLRMYH PYTAGGEAIY CHAKILIADE DVFRLGSSNM
NNRSLRLDTE CDLAIRASDE ATTKGIAAIR DGLIAEHLGV DVSVVSDLIA QTGSLIATIE
RLRGAGRTLQ PYEVPDLTSV EEWLADNEVL DPEGPAEMFE SLDKRGLFRR WRRRK
//