ID I8UJE8_9BACI Unreviewed; 482 AA.
AC I8UJE8;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 45.
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_01979 {ECO:0000313|EMBL:EIT86985.1};
OS Fictibacillus macauensis ZFHKF-1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Fictibacillus.
OX NCBI_TaxID=1196324 {ECO:0000313|EMBL:EIT86985.1, ECO:0000313|Proteomes:UP000004080};
RN [1] {ECO:0000313|EMBL:EIT86985.1, ECO:0000313|Proteomes:UP000004080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZFHKF-1 {ECO:0000313|EMBL:EIT86985.1,
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:EIT86985.1}.
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DR EMBL; AKKV01000019; EIT86985.1; -; Genomic_DNA.
DR RefSeq; WP_007200497.1; NZ_AKKV01000019.1.
DR AlphaFoldDB; I8UJE8; -.
DR STRING; 1196324.A374_01979; -.
DR PATRIC; fig|1196324.3.peg.394; -.
DR eggNOG; COG1502; Bacteria.
DR OrthoDB; 9762009at2; -.
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: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: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 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT TRANSMEM 36..54
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT DOMAIN 217..244
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 395..422
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT ACT_SITE 222
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 224
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 229
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 400
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 402
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 407
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
SQ SEQUENCE 482 AA; 55676 MW; BDCC56F0B6AF0669 CRC64;
MSTFTTLFIL GNTLNILLAA VIVFRERRDA SSTWAWLLVL VFIPIAGFIV YLFFGRNLNR
HRLFVWADRK KVGLEKTLKS QIEHIRDGSF EFTNEPERAS QDLIYMQLLN NEAPFTRDNY
IDIFTDGNEK FDALLRDITN ATEHIHLQYY IIKKDNLGKK VRDLLIEKAK QGVKVRVLYD
ELGSRTISKR FFHELRQHGG EVEVFFPSKF AFINFRLNYR NHRKIVIIDG VIGYVGGFNI
GDEYLGLDDM FGYWRDTHLR ITGTSVHSMQ MRFILDWNQA SDGHDIDYHP LLFPKPEQTG
NIGMQIITSG PDSEWPQIKD GYIKMISLAK KSITIQTPYF IPDASLLDTL RIACHSGVDV
RIMIPNKPDH LFVYWASLSN IGGLLKAGAK VYIYDNGFIH AKTMVVDDEI SSVGTANFDI
RSLKLNFEIN AFIYNKEIAK QLNGAFHEDI KLSRELTWEQ YLQRPTSVRF RESVSRLLSP
IL
//
