ID   CLSA_ERWT9              Reviewed;         486 AA.
AC   B2VKV4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 75.
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=ETA_15900;
OS   Erwinia tasmaniensis (strain DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB
OS   4357 / Et1/99).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=465817;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB 4357 / Et1/99;
RX   PubMed=18462403; DOI=10.1111/j.1462-2920.2008.01639.x;
RA   Kube M., Migdoll A.M., Mueller I., Kuhl H., Beck A., Reinhardt R.,
RA   Geider K.;
RT   "The genome of Erwinia tasmaniensis strain Et1/99, a non-pathogenic
RT   bacterium in the genus Erwinia.";
RL   Environ. Microbiol. 10:2211-2222(2008).
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; CU468135; CAO96636.1; -; Genomic_DNA.
DR   RefSeq; WP_012441329.1; NC_010694.1.
DR   AlphaFoldDB; B2VKV4; -.
DR   SMR; B2VKV4; -.
DR   STRING; 465817.ETA_15900; -.
DR   EnsemblBacteria; CAO96636; CAO96636; ETA_15900.
DR   KEGG; eta:ETA_15900; -.
DR   eggNOG; COG1502; Bacteria.
DR   HOGENOM; CLU_038053_1_0_6; -.
DR   OMA; TRFILDW; -.
DR   OrthoDB; 1881748at2; -.
DR   Proteomes; UP000001726; 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;
KW   Reference proteome; Repeat; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..486
FT                   /note="Cardiolipin synthase A"
FT                   /id="PRO_1000098907"
FT   TRANSMEM        3..23
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          219..246
FT                   /note="PLD phosphodiesterase 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT   DOMAIN          399..426
FT                   /note="PLD phosphodiesterase 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT   ACT_SITE        224
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT   ACT_SITE        226
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT   ACT_SITE        231
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT   ACT_SITE        404
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT   ACT_SITE        406
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
FT   ACT_SITE        411
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00190"
SQ   SEQUENCE   486 AA;  55097 MW;  3C598AD3B0E767CF CRC64;
     MTTFYTVMSW LLVFGYWLLI AGVTLRILMK RRAVPSAMAW LLIIYILPLV GIIAYLSLGE
     LHLGKRRAER ARTMWPSTAR WLNDLKSSHH IFAKENSDVA QALFQLCEKR QGIAGVKGNQ
     LQLLTSTDET LSTLVRDIEL ARHNIEMVFY IWQPGGHADD VAEALMAAAR RGVHCRLLLD
     SAGSVTFFRS PWPAMMRNAG VDVVEALRVS LLRVFLRRMD LRQHRKVVLI DNYIAYTGSM
     NLVDPRFFKQ NAGVGQWVDL MARMEGPVAT TMGIIYSCDW EIETGRRILP PPPDDNVMPF
     EQESGHTIQV IASGPGFPED MIHQALLTAV YSAREQLIMT TPYLVPSDDL LHAICTAAYR
     GVEVSIIVPR HIDSMLVRWA SRAFFGELLA AGVKIYQFEG GLLHSKSILV DGQLSLVGTV
     NLDMRSLWLN FEITLVIDDD GFGSDLARVQ EDYIARSRLV DAKRWAHRAY WQRIVERLFY
     FFSPLL