ID   CLSA_PSEPU              Reviewed;         481 AA.
AC   P31048;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Cardiolipin synthase A {ECO:0000255|HAMAP-Rule:MF_00190};
DE            Short=CL synthase {ECO:0000255|HAMAP-Rule:MF_00190};
DE            EC=2.7.8.- {ECO:0000255|HAMAP-Rule:MF_00190};
GN   Name=clsA {ECO:0000255|HAMAP-Rule:MF_00190}; Synonyms=cls;
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=G2;
RA   Lorenz D., Sokatch J.R.;
RL   Submitted (AUG-1992) to the EMBL/GenBank/DDBJ databases.
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_00190}.
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_00190};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00190}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00190}.
CC   -!- SIMILARITY: Belongs to the phospholipase D family. Cardiolipin synthase
CC       subfamily. ClsA sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_00190}.
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DR   EMBL; X55704; CAA39233.1; -; Genomic_DNA.
DR   AlphaFoldDB; P31048; -.
DR   SMR; P31048; -.
DR   STRING; 1240350.AMZE01000020_gene1468; -.
DR   eggNOG; COG1502; Bacteria.
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_00190; Cardiolipin_synth_ClsA; 1.
DR   InterPro; IPR022924; Cardiolipin_synthase.
DR   InterPro; IPR030840; CL_synthase_A.
DR   InterPro; IPR025202; PLD-like_dom.
DR   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   Pfam; PF13091; PLDc_2; 2.
DR   SMART; SM00155; PLDc; 2.
DR   TIGRFAMs; TIGR04265; bac_cardiolipin; 1.
DR   PROSITE; PS50035; PLD; 2.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Lipid biosynthesis; Lipid metabolism;
KW   Membrane; Phospholipid biosynthesis; Phospholipid metabolism; Repeat;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..481
FT                   /note="Cardiolipin synthase A"
FT                   /id="PRO_0000201261"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT   TRANSMEM        40..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT   DOMAIN          220..247
FT                   /note="PLD phosphodiesterase 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT   DOMAIN          394..421
FT                   /note="PLD phosphodiesterase 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT   ACT_SITE        225
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT   ACT_SITE        227
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT   ACT_SITE        232
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT   ACT_SITE        399
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT   ACT_SITE        401
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT   ACT_SITE        406
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
SQ   SEQUENCE   481 AA;  54329 MW;  B23A61677AE6D83F CRC64;
     MHMDYHSPYF FGYLLGLIHL LGVVAALHAL FTVRTAQGAI AWAMPLFFIP YLTLIPYLIF
     GARSFYAYIK ARRQANQEMH VAMANLNWRP WVEEALTARE SESYAALRAM PKLGRMPCLA
     NNQVKLLVNG KATFDAIFAA IEKARDVVLV QFFIIHDDTL GKALQQLLLR KAAEGVQVFV
     LYDRVGSHAL PASYSQQLRN GGVQIHAFAT RRGWFNRFQV NFRNHRKIVV VDGLLGFIGG
     HNVGDEYLGG HPQLSPWRDT HVQISGPVLA CLQESFAEDW YWATRQLPPL ILPDAYPDNG
     VLCQALASGP ADPQETCSLF FLEAIHSATR RVWITSPYFI PDEAVFAALR LAVLRGVDVR
     VLIPSRPDHR IVYAASSLFA FEAVRAGVRM FRYQPGFLHQ KVVLVDDEVS AIGSANLDNR
     SFRLNFEITL LTVDRNFADQ VEHMLIKDFE QAREITAEDS RDTHRLQQLG MRIARLISPI
     L