ID   CLS1_STAAR              Reviewed;         493 AA.
AC   Q6GH88;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 102.
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=SAR1328;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(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; BX571856; CAG40327.1; -; Genomic_DNA.
DR   RefSeq; WP_001160617.1; NC_002952.2.
DR   AlphaFoldDB; Q6GH88; -.
DR   SMR; Q6GH88; -.
DR   KEGG; sar:SAR1328; -.
DR   HOGENOM; CLU_038053_1_1_9; -.
DR   OMA; YVHVEFY; -.
DR   OrthoDB; 1881748at2; -.
DR   Proteomes; UP000000596; 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; Repeat; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..493
FT                   /note="Cardiolipin synthase 1"
FT                   /id="PRO_0000201271"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT   TRANSMEM        45..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT   DOMAIN          228..255
FT                   /note="PLD phosphodiesterase 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT   DOMAIN          406..433
FT                   /note="PLD phosphodiesterase 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT   ACT_SITE        233
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT   ACT_SITE        235
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT   ACT_SITE        240
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT   ACT_SITE        411
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT   ACT_SITE        413
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
FT   ACT_SITE        418
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01916"
SQ   SEQUENCE   493 AA;  56339 MW;  107AECE77CE93D19 CRC64;
     MQFSFSNDLG TLFTIILAIG FIINLVLAFI IIFLERNRRT ASSTWAWLFV LFVLPLIGFI
     LYLFFGRTVS ARKLNKNNGN VLTDFDGLLK QQIESFDKGN YGTDNKQVQK HHDLVRMLLM
     DQDGFLTENN KVDHFIDGND LYDQVLKDIK NAKEYIHLEY YTFALDGLGK RILHALEEKL
     KQGLEVKILY DDVGSKNVKM ANFDHFKSLG GEVEAFFASK LPLLNFRMNN RNHRKIIIID
     GQLGYVGGFN IGDEYLGLGK LGYWRDTHLR IQGDAVDALQ LRFILDWNSQ AHRPQFEYDV
     KYFPKKNGPL GNSPIQIAAS GPASDWHQIE YGYTKMIMSA KKSVYLQSPY FIPDNSYINA
     IKIAAKSGVD VHLMIPCKPD HPLVYWATFS NASDLLSSGV KIYTYENGFI HSKMCLIDDE
     IVSVGTANMD FRSFELNFEV NAFVYDENLA KDLRVAYEHD ITKSKQLTEE SYANRPLSVK
     FKESLAKLVS PIL