CLSB_SHIFL
ID CLSB_SHIFL Reviewed; 413 AA.
AC P59715;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 105.
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=SF0739, S0780;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN42374.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP16251.1; -; Genomic_DNA.
DR RefSeq; NP_706667.1; NC_004337.2.
DR AlphaFoldDB; P59715; -.
DR SMR; P59715; -.
DR STRING; 198214.SF0739; -.
DR EnsemblBacteria; AAN42374; AAN42374; SF0739.
DR EnsemblBacteria; AAP16251; AAP16251; S0780.
DR GeneID; 1023712; -.
DR KEGG; sfl:SF0739; -.
DR KEGG; sfx:S0780; -.
DR PATRIC; fig|198214.7.peg.860; -.
DR HOGENOM; CLU_038053_0_0_6; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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_0000201288"
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 388..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..413
FT /note="Polar residues"
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"
FT CONFLICT 133
FT /note="S -> A (in Ref. 2; AAP16251)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 413 AA; 47636 MW; 370F85AAECDE1BA0 CRC64;
MKCSWREGNK IQLLENGEQY YPAVFKAIGE AQERIILETF IWFEDNVGKQ LHAALLAAAQ
RGVKAEVLLD GYGSPDLSDE FVNELTAAGV VFRYYDPRPR LFGMRTNVFR RMHRKIVVID
ARIAFIGGLN YSSEHMSSYG PEAKQDYAVR LEGPIVEDIL QFELENLPGQ SAARRWWRRH
HKAEENRQPG EAQVLLVWRD NEEHRDDIER HYLKMLTQAQ REVIIANAYF FPGYRFLHAL
RKAARRGVRI KLIIQGEPDM PIVRVGARLL YNYLVKGGVQ VFEYRRRPLH GKVALMDDHW
ATVGSSNLDP LSLSLNLEAN VIIHDRHFNQ TLRDNLNGII AADCQQVDET MLPKRTWWNL
TKSVLAFHFL RHFPALVGWL PAHTPRLTQV DPPAQPTMET QDRVETENTG VNP
