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
//