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Database: UniProt
Entry: A0A2T7UV94_9RHOB
LinkDB: A0A2T7UV94_9RHOB
Original site: A0A2T7UV94_9RHOB 
ID   A0A2T7UV94_9RHOB        Unreviewed;       477 AA.
AC   A0A2T7UV94;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Phospholipase D {ECO:0000256|ARBA:ARBA00018392};
DE   AltName: Full=Choline phosphatase {ECO:0000256|ARBA:ARBA00029594};
GN   ORFNames=DDE23_05370 {ECO:0000313|EMBL:PVE48489.1};
OS   Pararhodobacter aggregans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Pararhodobacter.
OX   NCBI_TaxID=404875 {ECO:0000313|EMBL:PVE48489.1, ECO:0000313|Proteomes:UP000244810};
RN   [1] {ECO:0000313|EMBL:PVE48489.1, ECO:0000313|Proteomes:UP000244810}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D1-19 {ECO:0000313|EMBL:PVE48489.1,
RC   ECO:0000313|Proteomes:UP000244810};
RX   PubMed=21959289; DOI=10.1016/j.syapm.2011.08.006;
RA   Foesel B.U., Drake H.L., Schramm A.;
RT   "Defluviimonas denitrificans gen. nov., sp. nov., and Pararhodobacter
RT   aggregans gen. nov., sp. nov., non-phototrophic Rhodobacteraceae from the
RT   biofilter of a marine aquaculture.";
RL   Syst. Appl. Microbiol. 34:498-502(2011).
CC   -!- FUNCTION: Could be a virulence factor. {ECO:0000256|ARBA:ARBA00003145}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Secreted
CC       {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:PVE48489.1}.
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DR   EMBL; QDDR01000002; PVE48489.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T7UV94; -.
DR   OrthoDB; 9762009at2; -.
DR   Proteomes; UP000244810; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030572; F:phosphatidyltransferase activity; IEA:UniProt.
DR   GO; GO:0032049; P:cardiolipin biosynthetic process; IEA:UniProt.
DR   CDD; cd09158; PLDc_EcCLS_like_2; 1.
DR   Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR   InterPro; IPR027379; CLS_N.
DR   InterPro; IPR025202; PLD-like_dom.
DR   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   PANTHER; PTHR21248; CARDIOLIPIN SYNTHASE; 1.
DR   PANTHER; PTHR21248:SF22; PHOSPHOLIPASE D; 1.
DR   Pfam; PF13091; PLDc_2; 2.
DR   Pfam; PF13396; PLDc_N; 1.
DR   SMART; SM00155; PLDc; 2.
DR   SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR   PROSITE; PS50035; PLD; 2.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000244810};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        38..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          214..241
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          390..417
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
SQ   SEQUENCE   477 AA;  50221 MW;  1504F277BFE225A3 CRC64;
     METGFWVGVA LSLHYALQIA VLIRALTRPD REPASRVAWV LVILGIPAAG IALYLMLGEV
     SPGRRRVARM RAVRQALPVA VPGQGAASLP APARAAFGRG AAVNGFSPVG GNRAELAADA
     DAAIAGIVAD IEAARESVHI LVYIWLDDGN GRALMAALAR AAARGVTCRA MVDGLGSRGV
     LKSAAWAAMK AAGVRTGIAF DTRWAAARLL LGRIDIRNHR KIFVIDGRIA WCGSQNCADP
     AFLPKARFAP WVDIMLRIEG PVAWQTQALF AADWMAQGGD DITGALAGAP ATPEGGFPAL
     VVGTGPDLSA NAVPDMVALL LAAAEREVVI STPYFVPTQG LDEAIRATAL RGVSVTLILP
     ARNDSRMVAW ASRSTYAGLL RAGVAIHEFQ PGLLHAKTLT VDGGLAMIGS ANLDRRSFEL
     NFENVMLIAD APTCGLIRER QQVYLGQSRQ VSGDDVSGWS LPKRLLYNAA GIVSPVL
//
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