ID   CLS_GEOKA               Reviewed;         502 AA.
AC   Q5L1S5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 92.
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=GK0820;
OS   Geobacillus kaustophilus (strain HTA426).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   Geobacillus thermoleovorans group.
OX   NCBI_TaxID=235909;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTA426;
RX   PubMed=15576355; DOI=10.1093/nar/gkh970;
RA   Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA   Matsui S., Uchiyama I.;
RT   "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT   Geobacillus kaustophilus.";
RL   Nucleic Acids Res. 32:6292-6303(2004).
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; BA000043; BAD75105.1; -; Genomic_DNA.
DR   RefSeq; WP_011230321.1; NC_006510.1.
DR   AlphaFoldDB; Q5L1S5; -.
DR   SMR; Q5L1S5; -.
DR   STRING; 235909.GK0820; -.
DR   EnsemblBacteria; BAD75105; BAD75105; GK0820.
DR   KEGG; gka:GK0820; -.
DR   eggNOG; COG1502; Bacteria.
DR   HOGENOM; CLU_038053_1_1_9; -.
DR   OMA; HASRSYF; -.
DR   Proteomes; UP000001172; 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; Lipid biosynthesis; Lipid metabolism; Membrane;
KW   Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW   Repeat; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..502
FT                   /note="Cardiolipin synthase"
FT                   /id="PRO_1000058488"
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;  57433 MW;  B8F0473DDFAE54C4 CRC64;
     MRNTSRVAIL VVIVGALLAL TNGFWEGKLL GLFSVLMSCS VIFIALVISL ENRKPAQTIA
     WLAVLGSFPI VGFLFYLLFG RNYWQQRRYK KKADFDEAVL LKFQEPSPIA VERLPMAPHQ
     RPLLRLAYRI GQHPVSLASQ TAVLTNGEET FSSIFAELEK AEHHIHLEYY IVRHDEIGQQ
     LKRVLMEKAR QGVRVRFLYD AVGSWKLSNA YIEELRAAGV EMIPFSPVRL PFLSNQINFR
     NHRKIIVIDG GVGFVGGLNI GDEYLGKNKY FGFWRDTHLL IRGEAVRTLQ LIFLQDWYYM
     TGERLLTPDY LSPPLIVEEG QGGVQLIAGG PDQKWEVIKQ LYFAMITSAK RSIWVASPYF
     VPDEDILTAL KVAALSGIDV RLLAPKRPDK KIVFYASRSY FPELLEAGVK IYEYEKGFLH
     SKVIVVDGEL ASIGTANMDM RSFHLNFEVN AFLYYTDSIH KLVRDFLEDF RHASMIDYEQ
     FQQRPFRVRI AESVSRLLSP LL