ID R2RTX0_9ENTE Unreviewed; 491 AA.
AC R2RTX0;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 46.
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=UAS_01236 {ECO:0000313|EMBL:EOH86775.1};
OS Enterococcus asini ATCC 700915.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1158606 {ECO:0000313|EMBL:EOH86775.1, ECO:0000313|Proteomes:UP000013777};
RN [1] {ECO:0000313|EMBL:EOH86775.1, ECO:0000313|Proteomes:UP000013777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700915 {ECO:0000313|EMBL:EOH86775.1,
RC ECO:0000313|Proteomes:UP000013777};
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 asini ATCC_700915.";
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:EOH86775.1}.
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DR EMBL; AJAP01000012; EOH86775.1; -; Genomic_DNA.
DR RefSeq; WP_010753880.1; NZ_KB946294.1.
DR AlphaFoldDB; R2RTX0; -.
DR STRING; 57732.RU94_GL000672; -.
DR GeneID; 78365520; -.
DR PATRIC; fig|1158606.3.peg.1194; -.
DR eggNOG; COG1502; Bacteria.
DR HOGENOM; CLU_038053_1_1_9; -.
DR OrthoDB; 9762009at2; -.
DR Proteomes; UP000013777; 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:UP000013777};
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..30
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT DOMAIN 220..247
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 404..431
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT ACT_SITE 225
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 227
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 232
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 409
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 411
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 416
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
SQ SEQUENCE 491 AA; 56375 MW; FAF972181A5A16DD CRC64;
MEFQMEMSML NAALSLLILI NTIGAVITVF RRPRSITSIL AWLMTLTFFP VLGFIVYLFC
GRGIDGETVY RFDNEDQKRI GEINALIHEN NQEYHRSVNT TGSKLLERYL RNVEESPLAK
GNSIDLYTDG KEKFSALFED IRRAKDHIHV EYYAFFPDKI GTAFRDLLTE KAQSGVEVRL
IYDPWGAKGS GPSFFEPLVA AGGQVTAFIT SRDLIRKTRL NYHLHRKIVV IDGQIGWTGG
FNVGDQYLGE YERFGYWRDT HARIVGTASF TLQEIFLKDW NASVRKKGNQ LNYEDRYFVI
PSKEVGNVAI QVVSDGPENK VDILKSAFVK MLLAAEDKVW IQTPYLIPDD TMINALLIAA
QSGVDVRIMV PSMPDHPFIY RATQYYCNYL HQHGIKIYQY QKEGKGFLHA KTLVMDDTIC
SVGSTNQDIR SYSLNFEVSA FVYDEGTTLE MQRIFEKDME DCFLLTDEII TKQSRWLRFK
QNFSRLLSPI L
//
