ID A0A1L3K9I9_9LACO Unreviewed; 487 AA. AC A0A1L3K9I9; DT 12-APR-2017, integrated into UniProtKB/TrEMBL. DT 12-APR-2017, sequence version 1. DT 08-MAY-2019, entry version 7. 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 CC from one phosphatidylglycerol molecule to another to form CC cardiolipin (CL) (diphosphatidylglycerol) and glycerol. CC {ECO:0000256|HAMAP-Rule:MF_01916, ECO:0000256|SAAS:SAAS00006089}. 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; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01916, CC ECO:0000256|SAAS:SAAS01117805}; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP- CC Rule:MF_01916}; Multi-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_01916}. CC -!- SIMILARITY: Belongs to the phospholipase D family. Cardiolipin CC synthase subfamily. {ECO:0000256|HAMAP-Rule:MF_01916, CC ECO:0000256|SAAS:SAAS00538679}. 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 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|HAMAP-Rule:MF_01916, KW ECO:0000256|SAAS:SAAS00117509}; KW Complete proteome {ECO:0000313|Proteomes:UP000182202}; KW Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01916, KW ECO:0000256|SAAS:SAAS00006181}; KW Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01916, KW ECO:0000256|SAAS:SAAS00301903}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01916, KW ECO:0000256|SAAS:SAAS00016851}; KW Phospholipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01916, KW ECO:0000256|SAAS:SAAS00301877}; KW Phospholipid metabolism {ECO:0000256|HAMAP-Rule:MF_01916, KW ECO:0000256|SAAS:SAAS00006188}; KW Repeat {ECO:0000256|SAAS:SAAS00723978}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01916, KW ECO:0000256|SAAS:SAAS00420582}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_01916, KW ECO:0000256|SAAS:SAAS00420576}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01916, KW ECO:0000256|SAAS:SAAS00016984}. FT TRANSMEM 6 26 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01916}. FT TRANSMEM 38 56 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01916}. FT DOMAIN 216 243 PLD phosphodiesterase. FT {ECO:0000259|PROSITE:PS50035}. FT DOMAIN 400 427 PLD phosphodiesterase. FT {ECO:0000259|PROSITE:PS50035}. FT ACT_SITE 221 221 {ECO:0000256|HAMAP-Rule:MF_01916}. FT ACT_SITE 223 223 {ECO:0000256|HAMAP-Rule:MF_01916}. FT ACT_SITE 228 228 {ECO:0000256|HAMAP-Rule:MF_01916}. FT ACT_SITE 405 405 {ECO:0000256|HAMAP-Rule:MF_01916}. FT ACT_SITE 407 407 {ECO:0000256|HAMAP-Rule:MF_01916}. FT ACT_SITE 412 412 {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 //