ID   CLS_GEOSW               Reviewed;         502 AA.
AC   C5D794;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 68.
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=GWCH70_0766;
OS   Geobacillus sp. (strain WCH70).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   unclassified Geobacillus.
OX   NCBI_TaxID=471223;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WCH70;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Brumm P., Mead D.A., Richardson P.;
RT   "Complete sequence of chromosome of Geopacillus sp. WCH70.";
RL   Submitted (JUN-2009) 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: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; CP001638; ACS23652.1; -; Genomic_DNA.
DR   RefSeq; WP_012749451.1; NC_012793.1.
DR   AlphaFoldDB; C5D794; -.
DR   SMR; C5D794; -.
DR   STRING; 471223.GWCH70_0766; -.
DR   EnsemblBacteria; ACS23652; ACS23652; GWCH70_0766.
DR   KEGG; gwc:GWCH70_0766; -.
DR   eggNOG; COG1502; Bacteria.
DR   HOGENOM; CLU_038053_1_1_9; -.
DR   OMA; HASRSYF; -.
DR   OrthoDB; 1881748at2; -.
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..502
FT                   /note="Cardiolipin synthase"
FT                   /id="PRO_1000203995"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT   TRANSMEM        29..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT   TRANSMEM        59..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT   DOMAIN          237..264
FT                   /note="PLD phosphodiesterase 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT   DOMAIN          415..442
FT                   /note="PLD phosphodiesterase 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT   ACT_SITE        242
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT   ACT_SITE        244
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT   ACT_SITE        249
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT   ACT_SITE        420
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT   ACT_SITE        422
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT   ACT_SITE        427
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
SQ   SEQUENCE   502 AA;  57736 MW;  4E8EEAF9511CB207 CRC64;
     MRNTLRVIIF VLAVAAFLFL TNDYWEGKLL GGLSILISCS VVFIAFVISL ENRKPAHTIT
     WLVVLGSFPL IGFFFYLMFG RNYRKQRLFQ KKAMLDEQTF LKFQGQREWA IEQMPIGEHQ
     RPLLQLAHRI GKSPVSLATE TRVLTNGEET FSTIFEELEK ATHHIHLEYY IVRHDEVGQK
     LKTILIEKAK KGVHVRFLYD AVGSWKLSKT YIQELRDAGV EMIPFSPVRL PFLSNTINFR
     NHRKIIVIDG TIGFVGGLNI GDEYLGKDKY FGFWRDTHLW IRGEAVRTLQ LIFLQDWYYM
     TGKTLLTPEY LSPELVHYDG QGGVQLIAGG PDQKWEVIKH LYFAMITSAQ RSIWIASPYF
     VPDEDILTAL KIAALSGLDV RILAPKRPDK KIVFYASRSY FPELLEAGVK IYEYSKGFLH
     SKIMIVDGEL ASIGTANMDM RSFHLNFEVN AFLYHTDSTK KLVADFLEDL KEASPIDYET
     FQQRPLSIRV VESVSRLLSP LL