ID D1VRV6_9FIRM Unreviewed; 486 AA.
AC D1VRV6;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 24-JAN-2024, entry version 60.
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 Name=cls {ECO:0000313|EMBL:EFA90748.1};
GN ORFNames=HMPREF0628_1200 {ECO:0000313|EMBL:EFA90748.1};
OS Peptoniphilus lacrimalis 315-B.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Peptoniphilus.
OX NCBI_TaxID=596330 {ECO:0000313|EMBL:EFA90748.1, ECO:0000313|Proteomes:UP000005711};
RN [1] {ECO:0000313|EMBL:EFA90748.1, ECO:0000313|Proteomes:UP000005711}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=315-B {ECO:0000313|EMBL:EFA90748.1,
RC ECO:0000313|Proteomes:UP000005711};
RA Durkin A.S., Madupu R., Torralba M., Methe B., Sutton G., Strausberg R.L.,
RA Nelson K.E.;
RT "Genome Sequence of Peptoniphilus lacrimalis 315-B.";
RL Submitted (DEC-2009) 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:EFA90748.1}.
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DR EMBL; ADDO01000011; EFA90748.1; -; Genomic_DNA.
DR RefSeq; WP_004823855.1; NZ_ADDO01000011.1.
DR AlphaFoldDB; D1VRV6; -.
DR eggNOG; COG1502; Bacteria.
DR Proteomes; UP000005711; 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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}; Hydrolase {ECO:0000313|EMBL:EFA90748.1};
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:UP000005711};
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..33
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT DOMAIN 225..252
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 230
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 232
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 237
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; 56318 MW; A051F9B0C31581C7 CRC64;
MLKIYFDAIK SFAQFYSIIF LINIIFSAAV VFFQRKKPTS TLLWVMAINF LPIVGIILYL
LIGQDVSKSK MFDSKTQADR ITKNKYRDTI ENIQSREYKS SNAKTKEYKE IVKMFNNAEG
EILYSENDVK IFNNGVEKFK ALFEDIKNAK ESLYIQYYIF KSDQLSSQFI DLLIEKAKEG
LDVYLLVDGM GARHLKSSDR ERIRNAGVNF AVFFPGIFPK INTHINYRNH RKIAIIDRKI
GYVGGLNVGD EYVGNGKFGN WRDTHLRILG DAVNGLSWRF YLDYKFASKK DIKNFSTIYL
KENGNKDVSI VTSGPDTKAD SIRNGYEKLI TRAEKEIYIQ TPYFVPDEGL FKCLKVAALS
GVEVNIMIPQ KKDHPFVHWA SLSYVGELLD WGVNVYMYQK GFLHTKIMIS DDYLSSVGTA
NFDIRSFELN FEVNAFMFDY ELNQKLKEDF KNDLKDCKKI TKEIYEERGL FTKIREQTSR
LLSPLL
//
