ID C8S0X0_9RHOB Unreviewed; 658 AA.
AC C8S0X0;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Phospholipase D {ECO:0000256|ARBA:ARBA00018392};
DE AltName: Full=Choline phosphatase {ECO:0000256|ARBA:ARBA00029594};
GN ORFNames=Rsw2DRAFT_1698 {ECO:0000313|EMBL:EEW25411.1};
OS Rhodobacter sp. SW2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobacter.
OX NCBI_TaxID=371731 {ECO:0000313|EMBL:EEW25411.1, ECO:0000313|Proteomes:UP000010121};
RN [1] {ECO:0000313|EMBL:EEW25411.1, ECO:0000313|Proteomes:UP000010121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SW2 {ECO:0000313|EMBL:EEW25411.1,
RC ECO:0000313|Proteomes:UP000010121};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., Emerson D.;
RT "The draft genome of Rhodobacter sp. SW2.";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Could be a virulence factor. {ECO:0000256|ARBA:ARBA00003145}.
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:EEW25411.1}.
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DR EMBL; ACYY01000009; EEW25411.1; -; Genomic_DNA.
DR AlphaFoldDB; C8S0X0; -.
DR STRING; 371731.Rsw2DRAFT_1698; -.
DR eggNOG; COG1502; Bacteria.
DR OrthoDB; 8828485at2; -.
DR Proteomes; UP000010121; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030572; F:phosphatidyltransferase activity; IEA:UniProt.
DR GO; GO:0032049; P:cardiolipin biosynthetic process; IEA:UniProt.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR PANTHER; PTHR21248; CARDIOLIPIN SYNTHASE; 1.
DR PANTHER; PTHR21248:SF12; CARDIOLIPIN SYNTHASE C; 1.
DR Pfam; PF13091; PLDc_2; 1.
DR SMART; SM00155; PLDc; 1.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR PROSITE; PS50035; PLD; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000010121};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..658
FT /note="Phospholipase D"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002989764"
FT DOMAIN 574..601
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 658 AA; 72044 MW; 4897FB811E534A8C CRC64;
MRGPVAAMLA ALALMGGCAD PARTSANRLL NAQPTQGRVE AAYQAQLQAV VQGKPGAIAP
LTAGSLAAAP GPRLFQQRWR RAAADVYLDA TGPVAGAVFR FSGLQAADTA VTLHLNGPRA
LSLRGICDGP LQMRTADEER GVAAGRHFLL AMTNAAPDAT RLLLPPQTDT CNLAIGPLGK
PASYTLTLQR EELADPALAR LDQRYDLCTQ PSPRGLDPLE RAFFASGALS RSCTGPLGQA
DLLADPFDAF NAKIAALTGR RLTRAQIAAG NPEMPLDFSN APKLDLIYLS YLHLRADFSG
RLIFRALEYH AARGTPVRVL VTGHMTGGKS NTMLRELAAR YPLVQIQRFE WTPPALPAPR
DLLDRLHRGN HIKVFATLSA RPGQSHFMAS GRNLHDGFLF STPRDLSAFP ELYNYADRPK
SVAAFFSAYD DLDIDLRSDA TVRALMAQLS TFWHRDAATS VYRPFTLATE GPAPQTGMTH
FLSVPYVDGR ALERWYVALF DAARHSIDIV SPYMNLTPAL AAAFRRAEAR GVRVRFILPL
NMDNDPLGKQ KSDLNRLFVR EFVAEAALYE HIHPTNILHS KIVMIDGRLT ILGSVNFNQR
AFLHDTENGV AVLDPAFNRR LQPLFNEYLT DSVRLRGPGE ISFLVRFLSH SAFLRGLL
//
