ID A0A1L3K9I9_9LACO Unreviewed; 487 AA. AC A0A1L3K9I9; DT 12-APR-2017, integrated into UniProtKB/TrEMBL. DT 12-APR-2017, sequence version 1. DT 07-APR-2021, entry version 10. 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=LS838_00870 {ECO:0000313|EMBL:APG74029.1}; OS Lactobacillus delbrueckii subsp. sunkii. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1050107 {ECO:0000313|EMBL:APG74029.1, ECO:0000313|Proteomes:UP000182202}; RN [1] {ECO:0000313|EMBL:APG74029.1, ECO:0000313|Proteomes:UP000182202} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 17838 {ECO:0000313|EMBL:APG74029.1, RC ECO:0000313|Proteomes:UP000182202}; RA Jaros S., Januszkiewicz K., Wedrychowicz H.; RL Submitted (NOV-2016) 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP018217; APG74029.1; -; Genomic_DNA. DR RefSeq; WP_050951967.1; NZ_LGHR01000005.1. DR EnsemblBacteria; APG74029; APG74029; LS838_00870. DR Proteomes; UP000182202; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. 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 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 Pfam; PF13091; PLDc_2; 2. DR Pfam; PF13396; PLDc_N; 1. DR SMART; SM00155; PLDc; 2. DR TIGRFAMs; TIGR04265; bac_cardiolipin; 1. 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..26 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916" FT TRANSMEM 38..56 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916" FT DOMAIN 216..243 FT /note="PLD phosphodiesterase" FT /evidence="ECO:0000259|PROSITE:PS50035" FT DOMAIN 400..427 FT /note="PLD phosphodiesterase" FT /evidence="ECO:0000259|PROSITE:PS50035" FT ACT_SITE 221 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916" FT ACT_SITE 223 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916" FT ACT_SITE 228 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916" FT ACT_SITE 405 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916" FT ACT_SITE 407 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916" FT ACT_SITE 412 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916" SQ SEQUENCE 487 AA; 56200 MW; F5741C2C010B4763 CRC64; MTAISWIDIW HIIFFANAIL ALWTVFHRKR SVATSWAWLI VLIILPVVGF IIYGFVGRGI SQENLFAINR QKHIGLSNVQ KMITEAPAKI GQNDTSPSAH ILIKYLDKDQ ESPITKNNKL KLYTDGHDKF RDLFADIRQA KSSINVEYYT IYNDAIGNEF LKLLIQKAKE GVQVRVLYDA WGSFGASKSW FNQLTEAGGD VLPFITSRNM ISRNRINYHL HRKIVVIDGV TSWTGGFNVG DQYLGRKKKF GYWRDTHLRL VGSASLLLQE RFVMDWNASA VKEEELISFD EKLFPDLDEN DISKGDMAVQ VVSDGPDNDE PYMRNGLVRL MMLARKRVWI QTPYLIPDEA MIAAWQILAS SGVDLRIMIP CMPDHPFIYR ATQWYANQLV KIGVKVYTYN NGFMHAKTII VDDKYATVGS VNQDYRSYDL NFEDNVFVYD RAFNKEMSDQ FEKDMEQSTL LTPEIIKKQS HWLRFLQNFS RLLSPIL //