ID V7I1A2_9CLOT Unreviewed; 487 AA.
AC V7I1A2;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
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=T472_0219500 {ECO:0000313|EMBL:ETA78974.1};
OS Youngiibacter fragilis 232.1.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Youngiibacter.
OX NCBI_TaxID=994573 {ECO:0000313|EMBL:ETA78974.1, ECO:0000313|Proteomes:UP000017747};
RN [1] {ECO:0000313|EMBL:ETA78974.1, ECO:0000313|Proteomes:UP000017747}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=232.1 {ECO:0000313|EMBL:ETA78974.1,
RC ECO:0000313|Proteomes:UP000017747};
RX PubMed=24459265;
RA Wawrik C.B., Callaghan A.V., Stamps B.W., Wawrik B.;
RT "Genome Sequence of Youngiibacter fragilis, the Type Strain of the Genus
RT Youngiibacter.";
RL Genome Announc. 2:e01183-13(2014).
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:ETA78974.1}.
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DR EMBL; AXUN02000234; ETA78974.1; -; Genomic_DNA.
DR RefSeq; WP_023387036.1; NZ_AXUN02000234.1.
DR AlphaFoldDB; V7I1A2; -.
DR STRING; 994573.T472_0219500; -.
DR PATRIC; fig|994573.3.peg.3712; -.
DR eggNOG; COG1502; Bacteria.
DR OrthoDB; 9762009at2; -.
DR Proteomes; UP000017747; 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:UP000017747};
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 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT TRANSMEM 36..54
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT DOMAIN 206..233
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 400..427
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT ACT_SITE 211
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 213
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 218
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 405
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 407
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 412
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
SQ SEQUENCE 487 AA; 56625 MW; 980E2A5C1B89B5E4 CRC64;
MSLYNAVYII VILLNFIISV YIIFVNREKP EKSIGWLLIF MLVPIVGLVL YFLVGRNWRS
TNLKNRLSHE MLTLINASLD DYEGPYQDIA KLVTNGNSSP MFMKNEIKLY RDGFEKFNDL
LEDLKSARHH IHMEYYIVKS DDIGRKIFDI LKAKALEGVE VRFIMDKVGG RKFDRDYLRD
LIESGVEIVT YSAHFANFTR LIDTSINYRN HRKLVIIDGE IGYIGGNNIG DEYLGKSKFG
YWRDTHMRIR GDFVLGLQGL FYDDFFSVIN INENSRVFEL HRRKEVHKQI QDFEKYFPKT
SVSTYTPMQL AYCGPASPFS TIEQLFIKMI TSAREKIFIS SPYFIPSSGT LEALRIAILS
GVDVRIIMPE QYDHPPVQHA SMTYIKEILQ LGAKFYLYDK NSFIHTKAIV VDGRMFTMGT
ANFDVRSFYY NYEVNSVVYD ELEASKVEGM FFDDIARSRL ITLDEFNGRG LITNLKESFF
RVFSLLF
//
