ID U4QM09_LACHE Unreviewed; 485 AA.
AC U4QM09;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
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=LHCIRMBIA953_00730 {ECO:0000313|EMBL:CDI42719.1};
OS Lactobacillus helveticus CIRM-BIA 953.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=1226335 {ECO:0000313|EMBL:CDI42719.1, ECO:0000313|Proteomes:UP000017243};
RN [1] {ECO:0000313|EMBL:CDI42719.1, ECO:0000313|Proteomes:UP000017243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIRM-BIA 953 {ECO:0000313|EMBL:CDI42719.1,
RC ECO:0000313|Proteomes:UP000017243};
RA Valence F., Chuat V., Ma L., Creno S., Falentin H., Lortal S., Bizet C.,
RA Clermont D., Loux V., Bouchier C., Cousin S.;
RT "Draft Genome Sequence of five Lactobacillus helveticus strains CIRM-BIA
RT 101T, 103, 104, 951 and 953 isolated from milk product.";
RL Submitted (SEP-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:CDI42719.1}.
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DR EMBL; CBUH010000120; CDI42719.1; -; Genomic_DNA.
DR RefSeq; WP_023061573.1; NZ_CBUH010000120.1.
DR AlphaFoldDB; U4QM09; -.
DR Proteomes; UP000017243; 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}; 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 214..241
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 398..425
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT ACT_SITE 219
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 221
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 226
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 403
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 405
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 410
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
SQ SEQUENCE 485 AA; 56670 MW; 3071CDD696B1F86A CRC64;
MVWWHDFIRI IFITNTLLAF YIVFHRRRSV STTWAWLIIL LIFPVVGITL YAFFGRGISQ
ENIFSINKQH HIGLRNVQKS IAKAPKEVSP SDTSKLGEIA IHFFNRNNES PLTKNNNVEL
YTEGETFFHD LLKDMVRAKE TINVEFYTFY SDNIGNRVLQ LLIKKAKQGV KVRVIYDAWG
SMGATKAWFD QLRKAGGEVL PFITSRNMIT RYRINYHLHR KIVVIDGRIS WTGGFNIGDQ
YLGRKKKFGH WRDSQVRIVG SASLLLQERF VMDWNASIKC PEQLIRFNSA LFPDLDEKKI
HRGDVATQIA SDGPDRYIPY MRNGMMRLMQ LARKRLWIQT PYLIPDDAVF ATWQTIAMSG
VDVRIMIPCK PDHPFIYRAT QWYANELTRC GVKIYIYEDG FLHAKTTIID DSFSTVGSMN
QDYRSYDLNF EDNAIFYDKK FTKKMTEVFE ADMKKSHLLT REEIKKQGRI LRTLQSFSRM
LSPIL
//
