ID   CLS2_BACCR              Reviewed;         514 AA.
AC   Q81GK4;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Cardiolipin synthase 2 {ECO:0000255|HAMAP-Rule:MF_01916};
DE            Short=CL synthase 2 {ECO:0000255|HAMAP-Rule:MF_01916};
DE            EC=2.7.8.- {ECO:0000255|HAMAP-Rule:MF_01916};
GN   Name=cls2; OrderedLocusNames=BC_1191;
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; AAP08177.1; -; Genomic_DNA.
DR   RefSeq; NP_830976.1; NC_004722.1.
DR   RefSeq; WP_000799194.1; NZ_CP034551.1.
DR   AlphaFoldDB; Q81GK4; -.
DR   SMR; Q81GK4; -.
DR   STRING; 226900.BC_1191; -.
DR   EnsemblBacteria; AAP08177; AAP08177; BC_1191.
DR   GeneID; 67505909; -.
DR   KEGG; bce:BC1191; -.
DR   PATRIC; fig|226900.8.peg.1158; -.
DR   HOGENOM; CLU_038053_1_2_9; -.
DR   OMA; HASRSYF; -.
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..514
FT                   /note="Cardiolipin synthase 2"
FT                   /id="PRO_0000201244"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT   TRANSMEM        41..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT   TRANSMEM        71..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT   DOMAIN          249..276
FT                   /note="PLD phosphodiesterase 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT   DOMAIN          427..454
FT                   /note="PLD phosphodiesterase 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT   ACT_SITE        254
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT   ACT_SITE        256
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT   ACT_SITE        261
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT   ACT_SITE        432
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT   ACT_SITE        434
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT   ACT_SITE        439
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
SQ   SEQUENCE   514 AA;  59466 MW;  71CF854544BD69C7 CRC64;
     MKNTLKLIFF ILLLFALFVS LRMFIDVAFY SDVIGIKDVS ILGIISILFT VSAFLIGCVI
     FLENRHPSKT LTWLIVLGIF PVFGFFAYLL FGQNFRRKRM FQKKALLDEQ AFLQYKGHED
     YEERILRNHK HQELLFRLAD RLGALNISFQ TETRTLTNGD ETFRAILNGL KRAKHHIHME
     YYIVRDDKLG TEIKDILIQK SKEGVVVRFL YDAVGSFKLS KSYIEELNDA GVEMIPFFPV
     RFPILNDKIN YRNHRKIVVI DGNEGFVGGL NIGDEYLGKN KYFGFWRDTH LYLRGEAVQS
     LQLIFLQDWF YMTGEAVLAP EYLQAKAVEG DHWGGVQLVA GGPDNKWETI KHLYFAMIAS
     ARKSIWIATP YFIPDDDILS ALKVAALAGI DVRLLMPSKP DKRTVFYASR SYFPELLDAG
     VKIYEYEKGF LHSKIVIVDS DLASIGTANM DMRSFHLNFE VNAFLYDTDS IRKLVQDFKD
     DLEESSEIHG DHFHKRRLHR RIVESTYRLL SPLL