ID F0YZI1_9CLOT Unreviewed; 491 AA.
AC F0YZI1;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 56.
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=HMPREF0240_02156 {ECO:0000313|EMBL:EGB92836.1};
OS Clostridium sp. D5.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=556261 {ECO:0000313|EMBL:EGB92836.1, ECO:0000313|Proteomes:UP000003978};
RN [1] {ECO:0000313|EMBL:EGB92836.1, ECO:0000313|Proteomes:UP000003978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D5 {ECO:0000313|EMBL:EGB92836.1,
RC ECO:0000313|Proteomes:UP000003978};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Gevers D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., Chen Z., Engels R.,
RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E.R.,
RA Heiman D.I., Hepburn T.A., Howarth C., Jen D., Larson L., Mehta T.,
RA Park D., Pearson M., Richards J., Roberts A., Saif S., Shea T.D.,
RA Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J., Yandava C.,
RA Sibley C.D., White A.P., Crowley S., Surette M.G., Strauss J.C.,
RA Ambrose C.E., Allen-Vercoe E., Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Clostridium sp. D5.";
RL Submitted (MAR-2010) 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}.
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DR EMBL; GL870812; EGB92836.1; -; Genomic_DNA.
DR RefSeq; WP_009003485.1; NZ_GL870812.1.
DR AlphaFoldDB; F0YZI1; -.
DR eggNOG; COG1502; Bacteria.
DR HOGENOM; CLU_038053_1_1_9; -.
DR OrthoDB; 9762009at2; -.
DR Proteomes; UP000003978; 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:UP000003978};
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..34
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT TRANSMEM 41..63
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 404..431
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 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; 57113 MW; 8B6AB8269256D01D CRC64;
MAETIWNGLT TAYHFVMDNL AVINILLSLI IIFFQRRSPQ TVWTWLLLLY FIPILGFFLY
LVIGQDFHKS RMFKAKEIEG ELKYAVRRQE ETIYRKQLRL ANPEMARFKD LILYNLEAGE
SVLTDNNDVR IYTDGKEKFR ALIEEMKQAQ RYIHMQYYII RNDELWQEIE PVLTEKAKEG
VEVRVLFDSM GCRTMHNKDW ERLEKAGVQV AEFFPALLGQ LQLRVNYRNH RKIVVIDGRV
GFVGGFNVGR EYLGLDKKFG YWRDTHLCIE GAAVTSLAVR FVLDWNYAAR ENLFLEDHLF
EIPAYVRNGH DPVQIISSGP DSQTKTIHDN YLRLIHSAKD HVYLQTPYFI PDDSILDALK
IASRSGVDVR IMVPCKPDHP FVYWATYSYL GDMVAAGAKC YVYNNGFLHA KTLSVDGMVA
CVGTANMDIR SFGLNFEVNA VVYSERTVQR MERAFENDMT KCTHVTRKVY DQRSLIIRIK
EQFSRLLSPL L
//
