ID R2SW11_9ENTE Unreviewed; 482 AA.
AC R2SW11;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
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=UAW_00567 {ECO:0000313|EMBL:EOH99415.1};
OS Enterococcus haemoperoxidus ATCC BAA-382.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1158608 {ECO:0000313|EMBL:EOH99415.1, ECO:0000313|Proteomes:UP000013858};
RN [1] {ECO:0000313|EMBL:EOH99415.1, ECO:0000313|Proteomes:UP000013858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-382 {ECO:0000313|EMBL:EOH99415.1,
RC ECO:0000313|Proteomes:UP000013858};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A.M., Gilmore M.S., Lebreton F., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Enterococcus haemoperoxidus BAA-382.";
RL Submitted (FEB-2013) 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:EOH99415.1}.
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DR EMBL; AJAR01000010; EOH99415.1; -; Genomic_DNA.
DR RefSeq; WP_010760777.1; NZ_KE136479.1.
DR AlphaFoldDB; R2SW11; -.
DR STRING; 155618.RV06_GL001656; -.
DR PATRIC; fig|1158608.3.peg.545; -.
DR eggNOG; COG1502; Bacteria.
DR OrthoDB; 9762009at2; -.
DR Proteomes; UP000013858; 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}; 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 7..25
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT TRANSMEM 37..55
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT DOMAIN 218..245
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 395..422
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT ACT_SITE 223
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 225
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 230
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 400
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 402
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 407
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
SQ SEQUENCE 482 AA; 55894 MW; D860CADC66C29098 CRC64;
MKFLYENIFV IIFIANMLLS LVIVFRERKQ TAQTWSWLLV LMFIPVLGFI LYIFLGRGIS
KDKIFDMKMQ AKIGMNAEIE SEKQSLLRGL FPHPPTGEVD SKQLIYMLTV FESSLYTTNN
EIRLYTDGRE KFDGLIEDIR QATEHIHMEY YIYRGDTLGK EIRQELINAV KRGVKVRLLL
DAWGSTQVNM KFFEELKKIG GEIAFFFPLF VPYLNPRINY RNHRKIVVID GKIGYTGGFN
VGNEYLGEVE KFGYWRDNHL RIHGEAVYSL QNRFLMDWNS QHRKELSYDS TYFPPICSIG
KKAVQVVTSG PDSEHEQIKM TYLKMISIAK KEILIQTPYY IPDASIHEAL KLALLSGVKV
RIQIPNKPDH ILVYWATYSF SAELLEYGAI IETYEHGFIH AKTMIIDGGI VSVGSANIDV
RSFRLDFEVN TIIYDQEFSK EVRDAFYEDS KVSELLTEEK YRNRGVLIKL KEGLARLISP
LL
//
