ID   CLS1_BACCR              Reviewed;         509 AA.
AC   Q81I00;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=Cardiolipin synthase 1 {ECO:0000255|HAMAP-Rule:MF_01916};
DE            Short=CL synthase 1 {ECO:0000255|HAMAP-Rule:MF_01916};
DE            EC=2.7.8.- {ECO:0000255|HAMAP-Rule:MF_01916};
GN   Name=cls1; OrderedLocusNames=BC_0626;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC   / NCTC 2599 / NRRL B-3711;
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(2003).
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; AE016877; AAP07643.1; -; Genomic_DNA.
DR   RefSeq; NP_830442.1; NC_004722.1.
DR   RefSeq; WP_000743034.1; NZ_CP034551.1.
DR   AlphaFoldDB; Q81I00; -.
DR   SMR; Q81I00; -.
DR   STRING; 226900.BC_0626; -.
DR   PRIDE; Q81I00; -.
DR   EnsemblBacteria; AAP07643; AAP07643; BC_0626.
DR   KEGG; bce:BC0626; -.
DR   PATRIC; fig|226900.8.peg.585; -.
DR   HOGENOM; CLU_038053_1_2_9; -.
DR   OMA; YAPWVDI; -.
DR   Proteomes; UP000001417; 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..509
FT                   /note="Cardiolipin synthase 1"
FT                   /id="PRO_0000201243"
FT   TRANSMEM        4..24
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          422..449
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        427
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT   ACT_SITE        429
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT   ACT_SITE        434
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
SQ   SEQUENCE   509 AA;  58193 MW;  BC593C235250EEF9 CRC64;
     MKKPIVQLLL IFTIVSIVLF LLNTSYISLY TFVGALWSIT IVGISFVIFI ENRSPQSTLA
     WFLVLALLPI IGVLLYAIFG RSRWRRKKHL HRSEEQRKLF REILEGRRLE LLLTVPLNER
     SIHLTEVIQK FGGGPAADRT TTKLLTNGDQ TFSEILRAIE QAKHHIHIQY YIYKSDEIGT
     KVRDALIQKA KDGVIVRFLY DGLGSNTLRR RFLQPMKEAG IEIVEFDPIF SAWLLETVNY
     RNHRKIVIVD GEIGFTGGLN VGDEYLGRSK KFPVWRDSHL KIEGKALYKL QAIFLEDWLY
     ASSGLNTYSW DQFMNRQYFP GKEISNAEGA VQIVASGPSS DDKSIRNTLL AVMGSAKKSI
     WIATPYFIPD QETLTLLRLS AIAGIDVRIL YPGKSDSIIS DQASQSYFTP LLKAGASIYS
     YKDGFMHAKI VLVDDTIATI GTANMDVRSF ELNYEIISVL YESKTVHDIK RDFEEDFKHS
     TEIKWNSFQK RSIKKRILES FMRLISPLL