ID   CLSB_ECOL6              Reviewed;         413 AA.
AC   Q8FJN9;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Cardiolipin synthase B {ECO:0000255|HAMAP-Rule:MF_01917};
DE            Short=CL synthase {ECO:0000255|HAMAP-Rule:MF_01917};
DE            EC=2.7.8.- {ECO:0000255|HAMAP-Rule:MF_01917};
GN   Name=clsB {ECO:0000255|HAMAP-Rule:MF_01917}; Synonyms=ybhO;
GN   OrderedLocusNames=c0872;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Catalyzes the phosphatidyl group transfer from one
CC       phosphatidylglycerol molecule to another to form cardiolipin (CL)
CC       (diphosphatidylglycerol) and glycerol. {ECO:0000255|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:0000255|HAMAP-
CC         Rule:MF_01917};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01917};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01917}.
CC   -!- SIMILARITY: Belongs to the phospholipase D family. Cardiolipin synthase
CC       subfamily. ClsB sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_01917}.
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DR   EMBL; AE014075; AAN79345.1; -; Genomic_DNA.
DR   RefSeq; WP_000650340.1; NC_004431.1.
DR   AlphaFoldDB; Q8FJN9; -.
DR   SMR; Q8FJN9; -.
DR   STRING; 199310.c0872; -.
DR   EnsemblBacteria; AAN79345; AAN79345; c0872.
DR   KEGG; ecc:c0872; -.
DR   eggNOG; COG1502; Bacteria.
DR   HOGENOM; CLU_038053_0_0_6; -.
DR   OMA; EYCQRPL; -.
DR   BioCyc; ECOL199310:C0872-MON; -.
DR   Proteomes; UP000001410; 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   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   Pfam; PF13091; PLDc_2; 2.
DR   SMART; SM00155; PLDc; 2.
DR   PROSITE; PS50035; PLD; 2.
PE   3: Inferred from homology;
KW   Cell membrane; Lipid biosynthesis; Lipid metabolism; Membrane;
KW   Phospholipid biosynthesis; Phospholipid metabolism; Repeat; Transferase.
FT   CHAIN           1..413
FT                   /note="Cardiolipin synthase B"
FT                   /id="PRO_0000201285"
FT   DOMAIN          108..135
FT                   /note="PLD phosphodiesterase 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01917"
FT   DOMAIN          285..312
FT                   /note="PLD phosphodiesterase 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01917"
FT   REGION          390..413
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        113
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01917"
FT   ACT_SITE        115
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01917"
FT   ACT_SITE        120
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01917"
FT   ACT_SITE        290
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01917"
FT   ACT_SITE        292
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01917"
FT   ACT_SITE        297
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01917"
SQ   SEQUENCE   413 AA;  47552 MW;  21F9ED2C7CD24CA3 CRC64;
     MKCSWREGNK IQLLENGEQY YPAVFKAIGE AQERIILETF IWFEDDVGKQ LHAALLAAAQ
     RGVKAEVLLD GYGSPDLSDE FVNELTAAGV VFRYYDPRPR LFGMRTNVFR RMHRKIVVID
     ARIAFIGGLN YSAEHMSSYG PEAKQDYAVR LEGPIVEDIL QFELENLPGQ SAARRWWRRH
     HKAEENRQPG EAQVLLVWRD NEEHRDDIER HYLKMLTQAR REVIIANAYF FPGYRFLHAL
     RKAARRGVRI KLIIQGEPDM PIVRVGARLL YNYLVKGGVQ VFEYRRRPLH GKVALMDDHW
     ATVGSSNLDP LSLSLNLEAN VIIHDRNFNQ TLRDNLNGII AADCQQVDET MLPKRTWWNL
     TKSVLAFHFL RHFPALVGWL PAHTPRLAQV GPPAQPTMET QDRVETENTG VKP