ID   CLSA_PSEU2              Reviewed;         479 AA.
AC   Q4ZL66;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   25-MAY-2022, entry version 86.
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;
GN   OrderedLocusNames=Psyr_5079;
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a;
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT   syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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; CP000075; AAY40106.1; -; Genomic_DNA.
DR   RefSeq; WP_003340260.1; NC_007005.1.
DR   RefSeq; YP_238144.1; NC_007005.1.
DR   AlphaFoldDB; Q4ZL66; -.
DR   SMR; Q4ZL66; -.
DR   STRING; 205918.Psyr_5079; -.
DR   EnsemblBacteria; AAY40106; AAY40106; Psyr_5079.
DR   KEGG; psb:Psyr_5079; -.
DR   PATRIC; fig|205918.7.peg.5239; -.
DR   eggNOG; COG1502; Bacteria.
DR   HOGENOM; CLU_038053_1_0_6; -.
DR   OMA; TRFILDW; -.
DR   Proteomes; UP000000426; 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_00190; Cardiolipin_synth_ClsA; 1.
DR   InterPro; IPR022924; Cardiolipin_synthase.
DR   InterPro; IPR030840; CL_synthase_A.
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 inner membrane; Cell membrane; Lipid biosynthesis; Lipid metabolism;
KW   Membrane; Phospholipid biosynthesis; Phospholipid metabolism; Repeat;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..479
FT                   /note="Cardiolipin synthase A"
FT                   /id="PRO_1000077504"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT   TRANSMEM        38..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT   DOMAIN          218..245
FT                   /note="PLD phosphodiesterase 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT   DOMAIN          392..419
FT                   /note="PLD phosphodiesterase 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT   ACT_SITE        223
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT   ACT_SITE        225
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT   ACT_SITE        230
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT   ACT_SITE        397
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT   ACT_SITE        399
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT   ACT_SITE        404
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
SQ   SEQUENCE   479 AA;  53725 MW;  8702786B42763A66 CRC64;
     MDYHDPYFFG YVLGFIHLLG TGAAIHALLT VRTSQGAIAW AMPLLFIPYF TLLPYLVFGR
     SSFDAYIKAR RQANQEMRIA IGDLNWRPWM EEAVAARRSE AYAALRAMPK LGNMPALANN
     KVKLLINGEE TFGAIFQAIR EAKKTILVQF FIIHDDKLGR ELQSLLLEKA AEGVAIFVLY
     DRIGSHALPG AYIDKLRDGG VQIKAFATRG GWLNRFQINF RNHRKIVVVD GLKGYIGGHN
     VGDEYMGLKP PLAPWRDTHV QVIGPVVACL QESFAEDWFW ATRELPPLSL PDEFPEDGVL
     CQLLTSGPAD AQETCSLFFV EAIHAAEERV WITSPYFIPD EAVTAALTLA VLRGVDVRLL
     LPSRPDHYVV YAASSLYAFD AVRAGVRVFR YEPGFLHQKV VLVDNEITAI GSANLDNRSF
     RLNFELMLLT VDSDFSSQVE SMLTADFNLA REISVQESHE TRRLHQLGMR VARLISPIL