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Database: UniProt
Entry: D4S0U2_9FIRM
LinkDB: D4S0U2_9FIRM
Original site: D4S0U2_9FIRM 
ID   D4S0U2_9FIRM            Unreviewed;       508 AA.
AC   D4S0U2;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   SubName: Full=Phospholipase D domain protein {ECO:0000313|EMBL:EFF68440.1};
DE            EC=3.1.-.- {ECO:0000313|EMBL:EFF68440.1};
GN   ORFNames=BUTYVIB_01712 {ECO:0000313|EMBL:EFF68440.1};
OS   Butyrivibrio crossotus DSM 2876.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Butyrivibrio.
OX   NCBI_TaxID=511680 {ECO:0000313|EMBL:EFF68440.1, ECO:0000313|Proteomes:UP000006238};
RN   [1] {ECO:0000313|EMBL:EFF68440.1, ECO:0000313|Proteomes:UP000006238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2876 {ECO:0000313|EMBL:EFF68440.1,
RC   ECO:0000313|Proteomes:UP000006238};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:EFF68440.1}.
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DR   EMBL; ABWN01000030; EFF68440.1; -; Genomic_DNA.
DR   RefSeq; WP_005603463.1; NZ_GG663524.1.
DR   AlphaFoldDB; D4S0U2; -.
DR   STRING; 45851.BHV86_09255; -.
DR   eggNOG; COG1502; Bacteria.
DR   HOGENOM; CLU_038053_1_2_9; -.
DR   Proteomes; UP000006238; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008808; F:cardiolipin synthase activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032049; P:cardiolipin biosynthetic process; IEA:InterPro.
DR   CDD; cd09154; PLDc_SMU_988_like_1; 1.
DR   CDD; cd09160; PLDc_SMU_988_like_2; 1.
DR   Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR   InterPro; IPR022924; Cardiolipin_synthase.
DR   InterPro; IPR027379; CLS_N.
DR   InterPro; IPR025202; PLD-like_dom.
DR   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   NCBIfam; TIGR04265; bac_cardiolipin; 1.
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   Hydrolase {ECO:0000313|EMBL:EFF68440.1};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW   Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        38..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        68..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          244..271
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          421..448
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
SQ   SEQUENCE   508 AA;  58327 MW;  367374381B6F9ADA CRC64;
     MKRLFSPKKL RILFLALAVV VQAAVIVIPY VFLKHYIVHF NGVFRLVSVF VVLYILKSDI
     NPVYKIPWIV LLLALPVFGG VLYIIYGRLH FSKKDIMTFV DINNKCKEAL ALRPSANDSL
     EKEAPLIYPQ AKYLLDYALA PTYKNTETTY FPLGDDMFPV MLSELNKAEK FIFMEYFIIE
     DGLMLNSILD ILKEKASRGV DVRFMYDSLG SIAKAPVDIV RDLRKAGIRC FEFNTFRSIL
     DNRYNNRDHR KICVIDGNVG FTGGVNLADE YINVKTVYGH WKDTAIMIKG DAVWSLTNMF
     LTLWDGINKC DEDFRKYLPD IDVKTDNGYV IPYTDFPIDN ETVGKSVYLN MINRANRYIY
     IMTPYLILDN TMATSLCDAA KSGIDVRLIT PGIADKKLVN LLTKSYYDKL IEAGVKIYEY
     TPGFVHAKIF VSDDETAVVG TINLDYRSLA HHFENAIWMY KTDIVADIKK DFLDTQEKCE
     RITLEKCMKK SFAKIIFLPI LRLFSPML
//
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