ID A0A1G6ZWE6_PEPNI Unreviewed; 515 AA.
AC A0A1G6ZWE6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Cardiolipin synthase {ECO:0000313|EMBL:SDE06859.1};
GN ORFNames=SAMN04489866_11611 {ECO:0000313|EMBL:SDE06859.1};
OS Peptococcus niger.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Peptococcus.
OX NCBI_TaxID=2741 {ECO:0000313|EMBL:SDE06859.1, ECO:0000313|Proteomes:UP000198995};
RN [1] {ECO:0000313|EMBL:SDE06859.1, ECO:0000313|Proteomes:UP000198995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20475 {ECO:0000313|EMBL:SDE06859.1,
RC ECO:0000313|Proteomes:UP000198995};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; FNAF01000016; SDE06859.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6ZWE6; -.
DR STRING; 2741.SAMN04489866_11611; -.
DR OrthoDB; 9762009at2; -.
DR Proteomes; UP000198995; 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:UP000198995};
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..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 73..94
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 248..275
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 428..455
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 515 AA; 59565 MW; 392DCF686DF3BFFE CRC64;
MSKINTDKPK EVIMHPVGIM LIVLVLQVVL IIAGYLLLRN YLQIATVFWY ALAISLVIYL
LNKHQNPSYQ IAWIIIMCLM PIFGGLFFLT IQLIPGTRRL AERVSWRVRA TAKYLPQNKE
PVDSLRAHSA RFASLADYLY RVGVHPTYSH TETRYFPLGD DALPVMLEDM EKAQEYIFME
YFIVSEGKFW DAVFDVLKRK VAQGVTVRFM YDGTNMFSLP KDFQRRCIDA GINCRIFSPL
RPIFSTYQNN RDHRKIMVID GAVGYTGGIN LADEYINEED RFGHWKDTVI RLEGDAVMSM
LATFLQLWHV EEEDKADYQR WLDREPAVRH LEVANWVVPY ADAPEDGATL AQQVYMHILN
MATRYVHIMT PYLILDYEMV QALIFAARRG IDVAILMPHI PDKKIPFYIA RSFYPELIKN
GVRIIEYEPG FVHAKSFVSD DCVSVVGTVN LDYRSLYLHF ENGVLVYNDD FAAQVEADFQ
ASVAKGHEMT IHDYEITPWY QRATGRIMRI FGPLM
//
