ID A0A418NNI4_9SPHN Unreviewed; 469 AA.
AC A0A418NNI4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Phospholipase D {ECO:0000256|ARBA:ARBA00018392};
DE AltName: Full=Choline phosphatase {ECO:0000256|ARBA:ARBA00029594};
GN ORFNames=D2V07_16475 {ECO:0000313|EMBL:RIV83402.1};
OS Aurantiacibacter zhengii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Aurantiacibacter.
OX NCBI_TaxID=2307003 {ECO:0000313|EMBL:RIV83402.1, ECO:0000313|Proteomes:UP000286576};
RN [1] {ECO:0000313|EMBL:RIV83402.1, ECO:0000313|Proteomes:UP000286576}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V18 {ECO:0000313|EMBL:RIV83402.1,
RC ECO:0000313|Proteomes:UP000286576};
RA Fang C., Wu Y.-H., Sun C., Wang H., Cheng H., Meng F.-X., Wang C.-S.,
RA Xu X.-W.;
RT "Erythrobacter zhengii sp.nov., a bacterium isolated from deep-sea
RT sediment.";
RL Submitted (AUG-2018) 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:RIV83402.1}.
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DR EMBL; QXFL01000010; RIV83402.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A418NNI4; -.
DR OrthoDB; 8828485at2; -.
DR Proteomes; UP000286576; 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:UP000286576};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 97..124
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 311..338
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 126..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 469 AA; 54584 MW; F2CE3CDEA4118723 CRC64;
MLKARQRILL IGWDFDTRIH LKRGRRWWQK GWKSEYPSRL GSFIIWLNNH RPDLEIRILK
WSYGFLKFFG RGAMAFDLLR WWRHRRIDFK FDTAHPVACS HHQKLVIIDD DFAVCGGIDM
TTRRWDTREH LEDEPGRKRP DGTPYGPWHD LTMMMEGEVA SELERLGRAR WVRAGGKPLS
KPHPDPGSAW PDNLAPHFED VEVGIARTRA EYDKDPKVDE IETLFLRQIA GAKRFVYAEN
QYFTSRTICE AIAKRLSQPD PPEFTIVMPH TGEGWAEATA MDPARDELVA ALEELDTHDR
FNLYVPHSGE TPIYVHAKLM IVDDRILRVG SANMNNRSMG LDSECDVFID CDRPGNAKAE
PAIRAIRESL LSEHLGIFKQ DVSFLIEKHG SMAGMIDYIG DRNRRYLRRL RPARHEDWER
GLALDERLDP EQPEELFDFD KSDRGLFRRG SLLAKAHSKL KRRRKPANE
//
