ID   CLS_LISMH               Reviewed;         482 AA.
AC   B8DBK8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Cardiolipin synthase {ECO:0000255|HAMAP-Rule:MF_01916};
DE            Short=CL synthase {ECO:0000255|HAMAP-Rule:MF_01916};
DE            EC=2.7.8.- {ECO:0000255|HAMAP-Rule:MF_01916};
GN   Name=cls; OrderedLocusNames=LMHCC_0097;
OS   Listeria monocytogenes serotype 4a (strain HCC23).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=552536;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HCC23;
RX   PubMed=21602330; DOI=10.1128/jb.05236-11;
RA   Steele C.L., Donaldson J.R., Paul D., Banes M.M., Arick T., Bridges S.M.,
RA   Lawrence M.L.;
RT   "Genome sequence of lineage III Listeria monocytogenes strain HCC23.";
RL   J. Bacteriol. 193:3679-3680(2011).
CC   -!- FUNCTION: Catalyzes the reversible phosphatidyl group transfer from one
CC       phosphatidylglycerol molecule to another to form cardiolipin (CL)
CC       (diphosphatidylglycerol) and glycerol. {ECO:0000255|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:0000255|HAMAP-
CC         Rule:MF_01916};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01916};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01916}.
CC   -!- SIMILARITY: Belongs to the phospholipase D family. Cardiolipin synthase
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01916}.
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DR   EMBL; CP001175; ACK38459.1; -; Genomic_DNA.
DR   RefSeq; WP_003729224.1; NC_011660.1.
DR   AlphaFoldDB; B8DBK8; -.
DR   SMR; B8DBK8; -.
DR   KEGG; lmh:LMHCC_0097; -.
DR   HOGENOM; CLU_038053_1_1_9; -.
DR   OMA; TRFILDW; -.
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; Lipid biosynthesis; Lipid metabolism; Membrane;
KW   Phospholipid biosynthesis; Phospholipid metabolism; Repeat; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..482
FT                   /note="Cardiolipin synthase"
FT                   /id="PRO_1000124269"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT   TRANSMEM        34..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT   DOMAIN          217..244
FT                   /note="PLD phosphodiesterase 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT   DOMAIN          395..422
FT                   /note="PLD phosphodiesterase 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT   ACT_SITE        222
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT   ACT_SITE        224
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT   ACT_SITE        229
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT   ACT_SITE        400
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT   ACT_SITE        402
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT   ACT_SITE        407
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
SQ   SEQUENCE   482 AA;  55348 MW;  E40E2ACED650756A CRC64;
     MGLLAYLLVI LLILNVFFAA VTVFLERRDT SATWAWLLVL TFVPIFGFII YLIFGRKLSG
     KKIFDWKGQE KIGIQESTAN QIEMIRQKEF PFSDPNVKKH RDLIYLLLVN DGAILTQDNE
     VELFVDGHEK FDALIADIEN AKDHIHLIYY IFHSDELGNR LMRVLERKAA EGLNVKIIYD
     AMGSRTTKKS FFRTFQKNGG LVRPFFPSKL PLINFRLNYR NHRKLAIIDG DVGYIGGFNI
     GDEYLGASKK FGYWRDTHLR VHGKAVYAMQ TRFIMDWNSA SSTHKIDYKA RYFPTFHGKG
     HTSMQIVSSG PDSEWQQIKN GYIKMINAAK KTIYLQSPYF IPDASLLEAI KIAALSGVDV
     RVMIPNKPDH AFVYRATTNY AGELMETGAK IFIYDNGFIH AKTLVVDGEI ASVGTANMDF
     RSFRLNFEVN AFIYEKQMVQ KLEDAFLEDI LKSYQLTPEL YAKRSLWIKF KEAVSRLLSP
     IL