ID A0A2T0BMT1_9CLOT Unreviewed; 507 AA.
AC A0A2T0BMT1;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Putative cardiolipin synthase YwiE {ECO:0000313|EMBL:PRR85190.1};
DE EC=2.7.8.- {ECO:0000313|EMBL:PRR85190.1};
GN Name=ywiE {ECO:0000313|EMBL:PRR85190.1};
GN ORFNames=CLLU_18340 {ECO:0000313|EMBL:PRR85190.1};
OS Clostridium luticellarii.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1691940 {ECO:0000313|EMBL:PRR85190.1, ECO:0000313|Proteomes:UP000237798};
RN [1] {ECO:0000313|EMBL:PRR85190.1, ECO:0000313|Proteomes:UP000237798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29923 {ECO:0000313|EMBL:PRR85190.1,
RC ECO:0000313|Proteomes:UP000237798};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Clostridium luticellarii DSM 29923.";
RL Submitted (MAR-2018) 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:PRR85190.1}.
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DR EMBL; PVXP01000022; PRR85190.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0BMT1; -.
DR OrthoDB; 9762009at2; -.
DR Proteomes; UP000237798; 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: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 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 Reference proteome {ECO:0000313|Proteomes:UP000237798};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PRR85190.1};
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..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 70..91
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 243..270
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 420..447
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 507 AA; 59524 MW; FB728009F8453E78 CRC64;
MGERKTFISI LKFIAFIFWL IFQFIAIALI FNIFNIFFIY YFIFFEFISA VSVIHLNYKD
KNTSYKISWI ALILLIPVVG VIIYILSRIG IKRNFNKMNK MELDEKIFPE ENESMLSMLK
SENKTRYNQT RLIKNISGYG VYFNTKINYF SSGESMYKSL LKELKKADKF IFLEYFIISR
GKMWDEIFEV LKEKAQSGVE VRILVDYIGS MFALPKDFEE SLKKNNIKYK IFNPIKILLN
VMLNYRDHRK IAVIDGKIAF TGGMNIGDEY INSYRKYGYW KDMGVCLEGN AVYSFTSMFL
RMWQSITKKR ENFRKYKFES EFNEYTGIVV PYNSSPEESN DVAQDVYLSI IDSAKDYIYI
TTPYLVIGYE MILALSLAAK RGVDVRILTP SIPDKKTIQI LTRSHYDKLL DSGVKIYEYT
PGFIHGKTFV SDGECAVVGT INMDYRSLYL HFECAVYMYD VPIIKDIYND FISTIKVSKK
IEKKTWEKRC FLKRVLESIL RMFAPLA
//
