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Database: UniProt
Entry: A6T6N2_KLEP7
LinkDB: A6T6N2_KLEP7
Original site: A6T6N2_KLEP7 
ID   A6T6N2_KLEP7            Unreviewed;       414 AA.
AC   A6T6N2;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   RecName: Full=Cardiolipin synthase B {ECO:0000256|HAMAP-Rule:MF_01917};
DE            Short=CL synthase {ECO:0000256|HAMAP-Rule:MF_01917};
DE            EC=2.7.8.- {ECO:0000256|HAMAP-Rule:MF_01917};
GN   Name=ybhO {ECO:0000313|EMBL:ABR76253.1};
GN   Synonyms=clsB {ECO:0000256|HAMAP-Rule:MF_01917};
GN   ORFNames=KPN_00817 {ECO:0000313|EMBL:ABR76253.1};
OS   Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=272620 {ECO:0000313|EMBL:ABR76253.1, ECO:0000313|Proteomes:UP000000265};
RN   [1] {ECO:0000313|EMBL:ABR76253.1, ECO:0000313|Proteomes:UP000000265}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700721 / MGH 78578 {ECO:0000313|Proteomes:UP000000265};
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [2] {ECO:0000313|EMBL:ABR76253.1, ECO:0000313|Proteomes:UP000000265}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700721 / MGH 78578 {ECO:0000313|Proteomes:UP000000265};
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 phosphatidyl group transfer from one
CC       phosphatidylglycerol molecule to another to form cardiolipin (CL)
CC       (diphosphatidylglycerol) and glycerol. {ECO:0000256|HAMAP-
CC       Rule:MF_01917}.
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:0000256|HAMAP-
CC         Rule:MF_01917};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01917};
CC       Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01917}.
CC   -!- SIMILARITY: Belongs to the phospholipase D family. Cardiolipin synthase
CC       subfamily. ClsB sub-subfamily. {ECO:0000256|HAMAP-Rule:MF_01917}.
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DR   EMBL; CP000647; ABR76253.1; -; Genomic_DNA.
DR   RefSeq; WP_002895730.1; NC_009648.1.
DR   AlphaFoldDB; A6T6N2; -.
DR   STRING; 272620.KPN_00817; -.
DR   PaxDb; 272620-KPN_00817; -.
DR   DNASU; 5341747; -.
DR   EnsemblBacteria; ABR76253; ABR76253; KPN_00817.
DR   KEGG; kpn:KPN_00817; -.
DR   HOGENOM; CLU_038053_0_0_6; -.
DR   Proteomes; UP000000265; Chromosome.
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   CDD; cd09110; PLDc_CLS_1; 1.
DR   CDD; cd09159; PLDc_ybhO_like_2; 1.
DR   Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR   HAMAP; MF_01917; Cardiolipin_synth_ClsB; 1.
DR   InterPro; IPR030872; Cardiolipin_synth_ClsB.
DR   InterPro; IPR025202; PLD-like_dom.
DR   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   PANTHER; PTHR21248; CARDIOLIPIN SYNTHASE; 1.
DR   PANTHER; PTHR21248:SF23; CARDIOLIPIN SYNTHASE B; 1.
DR   Pfam; PF13091; PLDc_2; 2.
DR   SMART; SM00155; PLDc; 2.
DR   SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR   PROSITE; PS50035; PLD; 2.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01917};
KW   Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01917};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01917};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01917};
KW   Phospholipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01917};
KW   Phospholipid metabolism {ECO:0000256|HAMAP-Rule:MF_01917};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01917}.
FT   DOMAIN          108..135
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          286..313
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   REGION          393..414
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        113
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT   ACT_SITE        115
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT   ACT_SITE        120
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT   ACT_SITE        291
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT   ACT_SITE        293
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT   ACT_SITE        298
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
SQ   SEQUENCE   414 AA;  47999 MW;  594D4E705670B65B CRC64;
     MKCRWQEGNR ITLLENGDQY YPALFAAIGR ASRRVILESF IWFEDEVGRR LHAVLLEAAR
     RGIQVEVLLD GYGSPDLSDE FVGELTAAGV IFRYYDPRPK LMGMRTNLFR RMHRKIVVID
     DTTAFVGGIN YSAEHMSDYG PEAKQDYAVQ VEGPVVLDIL QFELENLPNS ETARRWWRRR
     RHQPEINQTP GEAQALFVWR DNQDHRDDIE RHYLKMLTSA RREVIIANAY FFPGYRLLHA
     MRNAARRGVR VKLIVQGEPD IPIVKFGAHL LYHYLVKGGV QIYEYRRRPL HGKVALADDH
     WATVGSSNLD PLSLSLNLEA NLIIHDRVFN QTLRDNLNGL IARDCQRIDK TMLPKRNWWR
     LGVSVMAFHF LRHFPAWVGW LPAHTPRLAR VSPPVQPEIE TQDRVESPAR DNPL
//
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