ID   CLS_ALKPO               Reviewed;         503 AA.
AC   O66043; D3FV21;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 121.
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=BpOF4_01900;
OS   Alkalihalophilus pseudofirmus (strain ATCC BAA-2126 / JCM 17055 / OF4)
OS   (Bacillus pseudofirmus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalophilus.
OX   NCBI_TaxID=398511;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9443601; DOI=10.1016/s0005-2760(97)00086-6;
RA   Guo D., Tropp B.E.;
RT   "Cloning of the Bacillus firmus OF4 cls gene and characterization of its
RT   gene product.";
RL   Biochim. Biophys. Acta 1389:34-42(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-2126 / JCM 17055 / OF4;
RX   PubMed=21951522; DOI=10.1111/j.1462-2920.2011.02591.x;
RA   Janto B., Ahmed A., Ito M., Liu J., Hicks D.B., Pagni S., Fackelmayer O.J.,
RA   Smith T.A., Earl J., Elbourne L.D., Hassan K., Paulsen I.T., Kolsto A.B.,
RA   Tourasse N.J., Ehrlich G.D., Boissy R., Ivey D.M., Li G., Xue Y., Ma Y.,
RA   Hu F.Z., Krulwich T.A.;
RT   "Genome of alkaliphilic Bacillus pseudofirmus OF4 reveals adaptations that
RT   support the ability to grow in an external pH range from 7.5 to 11.4.";
RL   Environ. Microbiol. 13:3289-3309(2011).
CC   -!- FUNCTION: Catalyzes the reversible phosphatidyl group transfer from one
CC       phosphatidylglycerol molecule to another to form cardiolipin (CL)
CC       (diphosphatidylglycerol) and glycerol.
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; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the phospholipase D family. Cardiolipin synthase
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01916}.
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DR   EMBL; U88888; AAC05444.1; -; Genomic_DNA.
DR   EMBL; CP001878; ADC48447.1; -; Genomic_DNA.
DR   RefSeq; WP_012959725.1; NC_013791.2.
DR   AlphaFoldDB; O66043; -.
DR   SMR; O66043; -.
DR   STRING; 398511.BpOF4_01900; -.
DR   EnsemblBacteria; ADC48447; ADC48447; BpOF4_01900.
DR   KEGG; bpf:BpOF4_01900; -.
DR   eggNOG; COG1502; Bacteria.
DR   HOGENOM; CLU_038053_1_2_9; -.
DR   OMA; HASRSYF; -.
DR   OrthoDB; 1881748at2; -.
DR   BRENDA; 2.7.8.B10; 11863.
DR   Proteomes; UP000001544; 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..503
FT                   /note="Cardiolipin synthase"
FT                   /id="PRO_0000201246"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT   TRANSMEM        30..50
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          238..265
FT                   /note="PLD phosphodiesterase 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT   DOMAIN          416..443
FT                   /note="PLD phosphodiesterase 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT   ACT_SITE        243
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT   ACT_SITE        245
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT   ACT_SITE        250
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT   ACT_SITE        421
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT   ACT_SITE        423
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT   ACT_SITE        428
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
SQ   SEQUENCE   503 AA;  57907 MW;  E02447184E987AF3 CRC64;
     MKNRLNVLAF FALLFAALYI SRGFLQSWMV GTLSVVFTLS VIFIGIIIFF ENRHPTKTLT
     WLLVLAAFPV VGFFFYLMFG QNHRKSKRFS KKAIEDERAF QKIEGQRQLN EEQLKKMGGH
     QQLLFRLAHK LGKNPISFSS ETKVLTDGKE TYAHILQALK MAEHHIHLEY YIVRHDDLGN
     QIKDILISKA KEGVHVRFLY DGVGSWKLSK SYVEELRDAG VEMVSFSPVK LPFLTHTINY
     RNHRKIIVID GVVGFVGGLN IGDEYLGKDA YFGYWRDTHL YVRGEAVRTL QLIFLQDWHY
     QTGETILNQT YLSPSLSMTK GDGGVQMIAS GPDTRWEVNK KLFFSMITSA KKSIWIASPY
     FIPDDDILSA LKIAALSGID VRILVPNRPD KRIVFHASRS YFPELLEAGV KVYEYNRGFM
     HSKIIIVDHE IASIGTSNMD MRSFHLNFEV NAYLYRTSSV TKLVSDYVYD LEHSNQINFS
     LFKNRPFFHR LIESTSRLLS PLL