CLSB_ECO57
ID CLSB_ECO57 Reviewed; 413 AA.
AC P0AA85; P75771;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=Z1008, ECs0867;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG55160.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB34290.1; -; Genomic_DNA.
DR PIR; C90737; C90737.
DR PIR; D85587; D85587.
DR RefSeq; NP_308894.1; NC_002695.1.
DR RefSeq; WP_000650337.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AA85; -.
DR SMR; P0AA85; -.
DR STRING; 155864.EDL933_0910; -.
DR EnsemblBacteria; AAG55160; AAG55160; Z1008.
DR EnsemblBacteria; BAB34290; BAB34290; ECs_0867.
DR GeneID; 66670939; -.
DR GeneID; 917609; -.
DR KEGG; ece:Z1008; -.
DR KEGG; ecs:ECs_0867; -.
DR PATRIC; fig|386585.9.peg.981; -.
DR eggNOG; COG1502; Bacteria.
DR HOGENOM; CLU_038053_0_0_6; -.
DR OMA; EYCQRPL; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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; Reference proteome;
KW Repeat; Transferase.
FT CHAIN 1..413
FT /note="Cardiolipin synthase B"
FT /id="PRO_0000201284"
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; 47634 MW; 74998B2A1AD24A11 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 VIIHDRHFNQ TLRDNLNGII AADCQQVDET MLPKRTWWNL
TKSVLAFHFL RHFPALVGWL PAHTPRLAQV DPPAQPTMET QDRVETENTG VKP
