ID   CLSA_PSEP1              Reviewed;         479 AA.
AC   A5WB80;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   25-MAY-2022, entry version 83.
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=Pput_5272;
OS   Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=351746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700007 / DSM 6899 / BCRC 17059 / F1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.;
RT   "Complete sequence of Pseudomonas putida F1.";
RL   Submitted (MAY-2007) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000712; ABQ81390.1; -; Genomic_DNA.
DR   RefSeq; WP_012054132.1; NC_009512.1.
DR   AlphaFoldDB; A5WB80; -.
DR   SMR; A5WB80; -.
DR   STRING; 351746.Pput_5272; -.
DR   EnsemblBacteria; ABQ81390; ABQ81390; Pput_5272.
DR   KEGG; ppf:Pput_5272; -.
DR   eggNOG; COG1502; Bacteria.
DR   HOGENOM; CLU_038053_1_0_6; -.
DR   OMA; TRFILDW; -.
DR   OrthoDB; 1881748at2; -.
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..479
FT                   /note="Cardiolipin synthase A"
FT                   /id="PRO_1000118593"
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;  54127 MW;  EF4BF827B777685B CRC64;
     MDYHSPYFFG YLLGMIHLLG IVAALHALFT VRTAQGAIAW AMPLLFIPYL TLIPYLIFGA
     RSFYAYIKAR RQANQEMHVA MANLNWRPWV EEALTARESE SYAALRAMPK LGRMPCLANN
     QVKLLINGKA TFDAIFAAIE KARDVVLVQF FIIHDDTLGK ALQQLLLRKA AEGVQVFVLY
     DRVGSHALPA SYSQMLRDGG VQIHAFATRR GWFNRFQVNF RNHRKIVVVD GLLGFIGGHN
     VGDEYLGEHP QLSPWRDTHV QISGPVLACL QESFAEDWYW ATRQLPPLIL PDTYPDNGVL
     CQALASGPAD PQETCSLFFL EAIHSATRRV WITSPYFIPD EAVFAALRLA VLRGVDVRVL
     IPSRPDHRIV YAASSLFAFE AVRAGVRMFR YQPGFLHQKV VLVDDDVSAI GSANLDNRSF
     RLNFEITLLT VDRGFADQVE HMLHEDFEHA REITAEDTQD THRLQQLGMR IARLISPIL