ID   CLSA_BUCBP              Reviewed;         490 AA.
AC   Q89AL5;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 110.
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=bbp_253;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(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_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 membrane {ECO:0000255|HAMAP-Rule:MF_00190};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-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; AE016826; AAO26980.1; -; Genomic_DNA.
DR   RefSeq; WP_011091381.1; NC_004545.1.
DR   AlphaFoldDB; Q89AL5; -.
DR   SMR; Q89AL5; -.
DR   STRING; 224915.bbp_253; -.
DR   EnsemblBacteria; AAO26980; AAO26980; bbp_253.
DR   KEGG; bab:bbp_253; -.
DR   eggNOG; COG1502; Bacteria.
DR   HOGENOM; CLU_038053_1_0_6; -.
DR   OMA; TRFILDW; -.
DR   OrthoDB; 1881748at2; -.
DR   Proteomes; UP000000601; 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 membrane; Lipid biosynthesis; Lipid metabolism; Membrane;
KW   Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW   Repeat; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..490
FT                   /note="Cardiolipin synthase A"
FT                   /id="PRO_0000201251"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT   TRANSMEM        39..59
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          403..430
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        408
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT   ACT_SITE        410
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT   ACT_SITE        415
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
SQ   SEQUENCE   490 AA;  56646 MW;  7C16B9D17A273B4A CRC64;
     MINYLFTITT WLIIISYWFI IIIVTCRILS KRRAISSSAA WLLVIYIIPF IGICTWFLLE
     EPYLGTRKLK LIKSVWSKKN KHFNNLKSHN YIFENNNSEV ARSLFKLCKY RQGISGIKFN
     KLKLLKNTKD VIKNLVRDIY LAKNTIEIVF YIWKPGGLAD NVAIALIQSA KRGIKCRLML
     DSAGSLEFFR SKWVDMMQQS GIQIVEALKI NLLHFFFRRM DLRQHRKFIL IDNYITYIGS
     MNLVDPYLFK KSLGIGQWID LMTRIEGPIS TTMGAIYSCD WEVETGQQIS PKRVKNNLII
     PTYPIKECTS IVQVIASGPG FTEDMIHQAL LTAIYSAQQK LTMTTPYLVP SDDLLRAICT
     AAQRGVEVIL IIPKSHDSLL VKWASRVFFS ELLESGVKIY QFKKGLLHSK SVLVDKQLSL
     IGTVNLDMRS LWLNFEITLV IDDKNFGKSL AIIHNEYISH SSLLDPKLWK IRSYWKKIIE
     KLFYFLSPLL