ID A0A1X9TV11_9LACO Unreviewed; 487 AA. AC A0A1X9TV11; DT 30-AUG-2017, integrated into UniProtKB/TrEMBL. DT 30-AUG-2017, sequence version 1. DT 11-DEC-2019, entry version 11. 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=B9N98_06265 {ECO:0000313|EMBL:ARR37751.1}, LDE01_01390 GN {ECO:0000313|EMBL:BBL26842.1}; OS Lactobacillus delbrueckii subsp. delbrueckii. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=83684 {ECO:0000313|EMBL:ARR37751.1, ECO:0000313|Proteomes:UP000194365}; RN [1] {ECO:0000313|EMBL:ARR37751.1, ECO:0000313|Proteomes:UP000194365} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TUA4408L {ECO:0000313|EMBL:ARR37751.1}; RA Hebert E.M., Saavedra L., Molina D., Albarracin L., Egusa S., Tanaka N., RA Okada S., Villena J., Kitazawa H.; RT "Genome sequencing of Lactobacillus delbrueckii TUA4408L."; RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:BBL26842.1, ECO:0000313|Proteomes:UP000319966} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 3202 {ECO:0000313|EMBL:BBL26842.1, RC ECO:0000313|Proteomes:UP000319966}; RA Miura T., Furukawa M., Shimamura M., Ohyama Y., Yamazoe A., Kawasaki H.; RT "Complete genome sequence of Lactobacillus delbrueckii subsp. delbrueckii RT NBRC 3202."; RL Submitted (JUN-2019) 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, 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; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01916, ECO:0000256|SAAS:SAAS01117805}; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01916}; CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01916}. CC -!- SIMILARITY: Belongs to the phospholipase D family. Cardiolipin synthase CC 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; CP021136; ARR37751.1; -; Genomic_DNA. DR EMBL; AP019750; BBL26842.1; -; Genomic_DNA. DR RefSeq; WP_072546917.1; NZ_CP021136.1. DR BioCyc; GCF_001888945:G1FF2-144-MONOMER; -. DR Proteomes; UP000194365; Chromosome. DR Proteomes; UP000319966; 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 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, 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}; 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 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916" FT TRANSMEM 33..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; 56307 MW; A2469E1069571E09 CRC64; MTAISWIDIW HIIFFANAIL ALWTVFHRKR SVAASWAWLI VLIILPVVGF IIYVFVGRGI SQENLFAINR QKHIGLSNVQ KMITEAPAKI DQNDTSPSAH 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 LTPEMIKKQS RWLRFLQNFS RLLSPIL //