ID I8UG31_9BACI Unreviewed; 500 AA.
AC I8UG31;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 44.
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=A374_08134 {ECO:0000313|EMBL:EIT85788.1};
OS Fictibacillus macauensis ZFHKF-1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Fictibacillus.
OX NCBI_TaxID=1196324 {ECO:0000313|EMBL:EIT85788.1, ECO:0000313|Proteomes:UP000004080};
RN [1] {ECO:0000313|EMBL:EIT85788.1, ECO:0000313|Proteomes:UP000004080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZFHKF-1 {ECO:0000313|EMBL:EIT85788.1,
RC ECO:0000313|Proteomes:UP000004080};
RX PubMed=22887677; DOI=10.1128/JB.01049-12;
RA Cai L., Zhang T.;
RT "Genome of Bacillus macauensis ZFHKF-1, a Long-Chain-Forming Bacterium.";
RL J. Bacteriol. 194:4780-4780(2012).
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:EIT85788.1}.
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DR EMBL; AKKV01000024; EIT85788.1; -; Genomic_DNA.
DR AlphaFoldDB; I8UG31; -.
DR STRING; 1196324.A374_08134; -.
DR PATRIC; fig|1196324.3.peg.1669; -.
DR eggNOG; COG1502; Bacteria.
DR Proteomes; UP000004080; 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:UP000004080};
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..48
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT TRANSMEM 60..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 413..440
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 418
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 420
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 425
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
SQ SEQUENCE 500 AA; 57562 MW; D96C03C634CE607B CRC64;
MRRLLEFCFL FLLLACLIVI CFTSLSYGWK WSAASVYVAI IVWTLYSLML ENRTSHFTLV
WMYVLIFLPF IGYLFYLYSG QLYLKGQLFQ TKLKHDRKEL QLLAEKGTEP NYEALSETGA
CFAKSSQQLY MTMYHEHTHT DILVNGEETF TALKEKLLAA TSYIHMEYYT FRSDELGRSI
IDVLIQKAQE GIDVRFLFDG MGSLTFANRD IKRLKTAGVK VYPFLPIKHG FFNQKFNFRN
HRKIAIIDGK YGFTGGLNIG MEYLGANKKL GFWRDTHLLL QGEAVQALHA IFLLDWNYVT
NESLMQEHRY TESYSVAGNG SVQVVPSGPD TGQGVMSDLY YSMISCAKQS IWIATPYFVP
NEAIRTALRV AARKGIQVRV MVPENSDSFL TKYASRSYVP ELLRAGIEIY FYKKGFMHQK
VVLIDGELAS VGSANMDLRS FHLNFEVNVF LTGHQVVSEL HELYKMDIQD CEHISLKDFK
ERGRWERSKE SFARLFSGVL
//