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Database: UniProt
Entry: A3VFW9_9RHOB
LinkDB: A3VFW9_9RHOB
Original site: A3VFW9_9RHOB 
ID   A3VFW9_9RHOB            Unreviewed;       612 AA.
AC   A3VFW9;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=Phospholipase D {ECO:0000256|ARBA:ARBA00018392};
DE   AltName: Full=Choline phosphatase {ECO:0000256|ARBA:ARBA00029594};
GN   ORFNames=RB2654_06534 {ECO:0000313|EMBL:EAQ12745.1};
OS   Maritimibacter alkaliphilus HTCC2654.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Maritimibacter.
OX   NCBI_TaxID=314271 {ECO:0000313|EMBL:EAQ12745.1, ECO:0000313|Proteomes:UP000002931};
RN   [1] {ECO:0000313|EMBL:EAQ12745.1, ECO:0000313|Proteomes:UP000002931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2654 {ECO:0000313|EMBL:EAQ12745.1,
RC   ECO:0000313|Proteomes:UP000002931};
RX   PubMed=20729358; DOI=10.1128/JB.00873-10;
RA   Thrash J.C., Cho J.C., Ferriera S., Johnson J., Vergin K.L.,
RA   Giovannoni S.J.;
RT   "Genome sequences of Pelagibaca bermudensis HTCC2601T and Maritimibacter
RT   alkaliphilus HTCC2654T, the type strains of two marine Roseobacter
RT   genera.";
RL   J. Bacteriol. 192:5552-5553(2010).
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:EAQ12745.1}.
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DR   EMBL; AAMT01000007; EAQ12745.1; -; Genomic_DNA.
DR   RefSeq; WP_008329901.1; NZ_VNHV01000013.1.
DR   AlphaFoldDB; A3VFW9; -.
DR   STRING; 314271.RB2654_06534; -.
DR   eggNOG; COG1502; Bacteria.
DR   HOGENOM; CLU_446044_0_0_5; -.
DR   OrthoDB; 8828485at2; -.
DR   Proteomes; UP000002931; 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   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:UP000002931};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..612
FT                   /note="Phospholipase D"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002660336"
FT   DOMAIN          528..555
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
SQ   SEQUENCE   612 AA;  67217 MW;  F1805A4447D7E3E0 CRC64;
     MWGTARKRAG WAAVTALGLV LLAACTSNLP DRQTADGRRV DGAIFLAPTG PEQADARFDL
     PTGAWQTARV TLQSTTYRDQ AARVTCDAPV VVNGPEGRKW VRPGGHQRVT VPAKGQVPAR
     LELTSGVTTC RVTWADHAVT LTRPEVVAPS VAAVDRARGA CVSPPAGTLD PLAQAFYAHT
     ALSRTCALRP GPVEIVETPI DALAARLQAL TGATLRCAHL AEGNPDIRLD FSNAPKLDLI
     VLASLHVRAD YCGALIQQAM TWHAARGTPV RILATAALQT GKDRDFWNAL AARYPNVQIQ
     YYRWQPRGIA TPATEFAAFH RANHVKLLIA LSSEPGRSRL IMGGRNLHDG FFFAEPFEIE
     DHPELRSYDD EWRDGLAWFA TFEDVDLVIR EDATVRQIAA HFGKLWRRDA PGQVLRPASE
     PGRVGPVPTD GVMRHFISQP WADARALEVD FVRMIDAARR EVTIVTPFLY PPPAVDAALA
     RAQARGVDVT LIARLDSTEP SAPVTRALAK DYMNRRYRDF AIYDYVPTER MIHTKILVID
     GRLAMSSSVN MNARSFGQDT ENGLIFLDRA MAARLGALAE TYRQRARRID APLPLTPLER
     TLAAIPVIRP LF
//
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