ID I0BUX1_9BACL Unreviewed; 499 AA.
AC I0BUX1;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 54.
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=B2K_36655 {ECO:0000313|EMBL:AFH66168.1};
OS Paenibacillus mucilaginosus K02.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=997761 {ECO:0000313|EMBL:AFH66168.1, ECO:0000313|Proteomes:UP000007392};
RN [1] {ECO:0000313|EMBL:AFH66168.1, ECO:0000313|Proteomes:UP000007392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K02 {ECO:0000313|EMBL:AFH66168.1,
RC ECO:0000313|Proteomes:UP000007392};
RA Xiao B., Sun L., Xiao L., Lian B.;
RT "Complete genome sequence of Paenibacillus mucilaginosus K02.";
RL Submitted (JUN-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}.
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DR EMBL; CP003422; AFH66168.1; -; Genomic_DNA.
DR RefSeq; WP_013921374.1; NC_017672.3.
DR AlphaFoldDB; I0BUX1; -.
DR KEGG; pmw:B2K_36655; -.
DR PATRIC; fig|997761.3.peg.7389; -.
DR HOGENOM; CLU_038053_1_1_9; -.
DR OrthoDB; 9762009at2; -.
DR Proteomes; UP000007392; Chromosome.
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}; 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 20..40
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT TRANSMEM 47..69
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT DOMAIN 232..259
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 412..439
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT ACT_SITE 237
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 239
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 244
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 417
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 419
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 424
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
SQ SEQUENCE 499 AA; 56903 MW; B62C7FC8423A8D3B CRC64;
MLSLPAMPAL PEFWNGGLWN LFSTWLPVIN FILAIPIIFL ERRNIGVTWA WLMVLLFLPV
LGFLLYLVFG QNLARRQLYK MKRRSERVVR AVAHEQVYRI DKGSMEYRNA SAEAYQPLIH
LNLKSGHSIL TQNNEVTVLT EGREKFEALL AHLREARQHI HLLYYKISYD KIGSDLLTIL
VDKAQSGVKV RLLYDAIGSP GLPRKWARKL MRSGAEVYPF FPSLVPYLNL KINYRNHRKV
AVIDGKVGFI GGFNIGNEYL GLDPRIGHWR DTHLMLRGGS VYELQRYFLM DWSLASGQVM
PDKEQTAFFP PLERQPGSAA VQIVTSGPNT DRQQIKTALI KLIHEARDRI WLQTPYFVPD
ESVMTALKIA ALSGVDVRLM VPFKGDHRLV QWATQAHVGE LLQVGARCFQ YQRGFLHAKT
VVVDGKAASV GTANMDHRSF VLNFEINAFL YDEKTAGQLE AAFEKDLAYC REFTAELYKG
RGLLNRIMES MARLLSPIL
//
