ID A0A0A5FTF0_9BACI Unreviewed; 501 AA.
AC A0A0A5FTF0;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=N783_05865 {ECO:0000313|EMBL:KGX83184.1};
OS Pontibacillus marinus BH030004 = DSM 16465.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Pontibacillus.
OX NCBI_TaxID=1385511 {ECO:0000313|EMBL:KGX83184.1, ECO:0000313|Proteomes:UP000030403};
RN [1] {ECO:0000313|EMBL:KGX83184.1, ECO:0000313|Proteomes:UP000030403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BH030004 {ECO:0000313|EMBL:KGX83184.1,
RC ECO:0000313|Proteomes:UP000030403};
RA Huang J., Wang G.;
RL Submitted (AUG-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:KGX83184.1}.
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DR EMBL; AVPF01000139; KGX83184.1; -; Genomic_DNA.
DR RefSeq; WP_027448736.1; NZ_KE384336.1.
DR AlphaFoldDB; A0A0A5FTF0; -.
DR STRING; 1385511.GCA_000425225_02270; -.
DR eggNOG; COG1502; Bacteria.
DR OrthoDB; 9762009at2; -.
DR Proteomes; UP000030403; 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:SF20; CARDIOLIPIN SYNTHASE YWIE-RELATED; 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:UP000030403};
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 7..25
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT TRANSMEM 31..50
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT TRANSMEM 59..78
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT DOMAIN 236..263
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 414..441
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT ACT_SITE 241
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 243
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 248
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 419
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 421
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 426
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
SQ SEQUENCE 501 AA; 58211 MW; 2F9157EB9F252D4B CRC64;
MKPHIQLLLL TILGIALFFI LLIPLSFVFQ VIFGLIYIGA VFTISFYIML ERRSSTNTIL
WIFFIFFVPI IGYFFYIYSG QLSRQGILFQ DKRRKAQEVF RTEEPVPRIQ ATERLNEQQL
AVSKVIQSLA DTHVRTRGHV SILTNGQEAF PEIMEGLKKA KSFIHMEYYL FNSDETGYEI
MDILMEKARE GVKVRLLYDS AGSLKLKKKD VQKMKEAGVE VHVFLPIKTA LITQTFNFRN
HRKIIVIDND IAFVGGMNIG DEYRGISEEF PDWRDTHTVV KGMPIKELHL IFLIDWWYIT
KENIIEEFSR AVIPEPKEHN TDAQIVPSGP HNQHQIMRDV YNALINSAKE RIMIATPYFV
PSREIHSALR IAAQKGLEVK LLIPKPSDNW LTYYAGHSYF PELLEDGIQI YLYEKDFMHH
KIMIVDDHTV SVGTANMDLR SFYLNFEVNV IMYGGQPVEQ IIQNYHSDLE DSMKVDHDQF
MKRPLSEKTK EAIARMFAPL L
//
