ID A0A1G7QZW5_9BACL Unreviewed; 476 AA.
AC A0A1G7QZW5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=SAMN04488542_12433 {ECO:0000313|EMBL:SDG04056.1};
OS Fontibacillus panacisegetis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Fontibacillus.
OX NCBI_TaxID=670482 {ECO:0000313|EMBL:SDG04056.1, ECO:0000313|Proteomes:UP000198972};
RN [1] {ECO:0000313|EMBL:SDG04056.1, ECO:0000313|Proteomes:UP000198972}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 28129 {ECO:0000313|EMBL:SDG04056.1,
RC ECO:0000313|Proteomes:UP000198972};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01916}.
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DR EMBL; FNBG01000024; SDG04056.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7QZW5; -.
DR STRING; 670482.SAMN04488542_12433; -.
DR OrthoDB; 9762009at2; -.
DR Proteomes; UP000198972; 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:UP000198972};
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 30..51
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT DOMAIN 213..240
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 389..416
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT ACT_SITE 218
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 220
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 225
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 394
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 396
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 401
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
SQ SEQUENCE 476 AA; 54989 MW; 78EAA4F88D24BF99 CRC64;
MLWLVCILLG FIFQIATIII LEYRNPGKAI AWMFILFLFP IIGFILYYFV AQDYRKRKKV
RRRGPRLFQE VRATLRKQST IVNSAEDMHQ EEFRHQERLF GLLTHVSDSP ITGCNRTKVL
SDGEAAFSEM LEAMETAKHH IHMEFYIFRA DRIGTKFQNV MIRKVKEGVQ VRLICDGLGS
YHLPKSFVRN LQDHGVEVYM FLPPLIAVMD RRLNYRNHRK ILVVDGTVGF VGGMNVGDDY
LGLYEKMGYW RDTQLKIEGD AVYYLQSTFL GDWRLASGQR LFHQDFFPEH HCNTDEQVQI
LVSGPDQNGD VIQEVVFGAI SVAKKRIWIT SPYFIPDPSI YTGLLTAAVS GIEVIVILPY
QSDNRLVKLA SLSYVEELLR AGVKFYQYRK GFVHAKVLIV DDLLASVGTA NMDMRSFFYN
FEMTALMFDQ SPIQKLSRDF EQDIEDSSPI TLREFSRRSL RQKGAEKLAR LLSPLL
//