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Database: UniProt
Entry: A0A1C0YN37_9BACL
LinkDB: A0A1C0YN37_9BACL
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ID   A0A1C0YN37_9BACL        Unreviewed;       486 AA.
AC   A0A1C0YN37;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Cardiolipin synthase {ECO:0000256|HAMAP-Rule:MF_01916};
DE            Short=CL synthase {ECO:0000256|HAMAP-Rule:MF_01916};
DE            EC=2.7.8.- {ECO:0000256|HAMAP-Rule:MF_01916};
GN   ORFNames=A6M13_01585 {ECO:0000313|EMBL:OCS88563.1};
OS   Caryophanon tenue.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Caryophanon.
OX   NCBI_TaxID=33978 {ECO:0000313|EMBL:OCS88563.1, ECO:0000313|Proteomes:UP000093199};
RN   [1] {ECO:0000313|EMBL:OCS88563.1, ECO:0000313|Proteomes:UP000093199}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14152 {ECO:0000313|EMBL:OCS88563.1,
RC   ECO:0000313|Proteomes:UP000093199};
RA   Verma A., Pal Y., Krishnamurthi S.;
RT   "Caryophanon tenue genome sequencing.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible phosphatidyl group transfer from one
CC       phosphatidylglycerol molecule to another to form cardiolipin (CL)
CC       (diphosphatidylglycerol) and glycerol. {ECO:0000256|HAMAP-
CC       Rule:MF_01916}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) = a
CC         cardiolipin + glycerol; Xref=Rhea:RHEA:31451, ChEBI:CHEBI:17754,
CC         ChEBI:CHEBI:62237, ChEBI:CHEBI:64716; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01916};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01916};
CC       Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01916}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the phospholipase D family. Cardiolipin synthase
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01916}.
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:OCS88563.1}.
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DR   EMBL; MASJ01000001; OCS88563.1; -; Genomic_DNA.
DR   RefSeq; WP_066542356.1; NZ_MASJ01000001.1.
DR   AlphaFoldDB; A0A1C0YN37; -.
DR   STRING; 33978.A6M13_01585; -.
DR   OrthoDB; 9762009at2; -.
DR   Proteomes; UP000093199; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008808; F:cardiolipin synthase activity; IEA:InterPro.
DR   GO; GO:0032049; P:cardiolipin biosynthetic process; IEA:InterPro.
DR   CDD; cd09110; PLDc_CLS_1; 1.
DR   CDD; cd09112; PLDc_CLS_2; 1.
DR   Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR   HAMAP; MF_01916; Cardiolipin_synth_Cls; 1.
DR   InterPro; IPR030874; Cardiolipin_synth_Firmi.
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   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_01916};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW   Rule:MF_01916};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW   Rule:MF_01916};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01916};
KW   Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209,
KW   ECO:0000256|HAMAP-Rule:MF_01916};
KW   Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264, ECO:0000256|HAMAP-
KW   Rule:MF_01916}; Reference proteome {ECO:0000313|Proteomes:UP000093199};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01916};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_01916};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_01916}.
FT   TRANSMEM        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT   TRANSMEM        37..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT   DOMAIN          221..248
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          399..426
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   ACT_SITE        226
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT   ACT_SITE        228
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT   ACT_SITE        233
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT   ACT_SITE        404
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT   ACT_SITE        406
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT   ACT_SITE        411
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
SQ   SEQUENCE   486 AA;  56029 MW;  5958282998AB1282 CRC64;
     MGQLIQSLDL PGLILLISNM FFVLAVVFIE RKHPSSAWAW MFVLIFAPFI GFIGYLLLGR
     RLRKKHLYRF SGDKYMGLNQ LMTYQVAALK DNTYDFHDVA AAKHRDLIYM HLTHDEAVLT
     QDNDVTLYTD GHEKFAQLLR DIEQAKHHIH MQYYIFRHDD LGQQILRALE KKAKQGVEVR
     FLYDAIGSNK LFKRHLRALR EAGGFTEVFF PSVLPLFNPR LNFRNHRKIV IIDGTISYVG
     GFNVGNEYLG IDPTYGYWRD THSRIEGSAT HELQTRFLID WNMAAKHARV AYDEAYYPAI
     PRRGTTAVQI VSSGPDSDWD SIKNSYIKMI LSAKKYVYIQ TPYFVPDDAV MEAIRIASLT
     GVDVRIMIPA VPDHKIVYWA TMSYMDDLLR AGAKVDLYEK GFIHAKTVVI DDEVATCGTT
     NFDVRSFSLN FEVNAFFLSG EKAYEMRKIY ERDLGHSRAL TLADYENRSL KKRFQESIAR
     LISPIL
//
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