ID   CLSA_KLEP7              Reviewed;         486 AA.
AC   A6TAJ7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 77.
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=KPN78578_21570; ORFNames=KPN_02190;
OS   Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=272620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700721 / MGH 78578;
RG   The Klebsiella pneumonia Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA   Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL   Submitted (SEP-2006) 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; CP000647; ABR77618.1; -; Genomic_DNA.
DR   RefSeq; WP_002910077.1; NC_009648.1.
DR   AlphaFoldDB; A6TAJ7; -.
DR   SMR; A6TAJ7; -.
DR   STRING; 272620.KPN_02190; -.
DR   DNASU; 5341967; -.
DR   EnsemblBacteria; ABR77618; ABR77618; KPN_02190.
DR   KEGG; kpn:KPN_02190; -.
DR   HOGENOM; CLU_038053_1_0_6; -.
DR   OMA; TRFILDW; -.
DR   Proteomes; UP000000265; 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_1000058490"
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;  54770 MW;  00F66DE0C4F71F13 CRC64;
     MTTFYTVVNW LVILGYWLLI AGVTLRILMK RRAVPSAMAW LLIIYILPLV GIIAYLSFGE
     LHLGKRRAER ARAMWPSTAK WLNDLKACKH IFAEDNSPVA ESLFKLCERR QGIGGVKGNQ
     LQLLTESDDV MQALIRDIQL ARHNIEMVFY IWQPGGMADS VAESLMAAAR RGVHCRLMLD
     SAGSVAFFRS PWAAMMRNAG IEVVEALKVN LMRVFLRRMD LRQHRKMVMI DNYIAYTGSM
     NMVDPRYFKQ DSGVGQWIDL MARMEGPVAT SMGIVYSCDW EIETGKRILP PPPDVNIMPF
     EEASGHTIHT IASGPGFPED LIHQALLTAA YAAKEHLIMT TPYFVPSDDL LHAICTAAQR
     GVDVSIILPR KNDSLLVGWA SRAFFTELLA AGVKIYQFEG GLLHTKSVLV DGELSLVGTV
     NLDMRSLWLN FEITLVIDDA GFGSDLAAVQ DDYISRSRLL DARLWLKRPL WQRIAERLFY
     FFSPLL