CLSB_SALTI
ID CLSB_SALTI Reviewed; 413 AA.
AC Q8Z883;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 113.
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=STY0847, t2076;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(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; AL513382; CAD05259.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO69696.1; -; Genomic_DNA.
DR RefSeq; NP_455350.1; NC_003198.1.
DR RefSeq; WP_000649638.1; NZ_WSUR01000021.1.
DR AlphaFoldDB; Q8Z883; -.
DR SMR; Q8Z883; -.
DR STRING; 220341.16502026; -.
DR EnsemblBacteria; AAO69696; AAO69696; t2076.
DR KEGG; stt:t2076; -.
DR KEGG; sty:STY0847; -.
DR PATRIC; fig|220341.7.peg.852; -.
DR eggNOG; COG1502; Bacteria.
DR HOGENOM; CLU_038053_0_0_6; -.
DR OMA; EYCQRPL; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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_0000201286"
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 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; 47258 MW; 1F71EEFD90CCF463 CRC64;
MKCGWREGNQ IQLLENGDQF YPAVFEAIAQ AQQKIILETF ILFEDEVGKK LHAALLKAAQ
RGVKAEVLLD GYGSPDLSDA FVGELTSAGV IFRYYDPRPR LLGLRTNIFR RMHRKIVVID
DRIAFVGGIN YSAEHMSDYG PQAKQDYAVR VEGPVVADIL QFEVENLPGQ SPARRWWKRH
HQAEENRHPG EAQALFVWRD NEEHRDDIER HYLKMLTQAK REVIIANAYF FPGYRLLHAM
RKAARRGVSV KLIVQGEPDM PIVKVGARLL YNYLVKGGVQ VYEYRRRPLH GKVALMDDHW
ATVGSSNLDP LSLSLNLEAN LIIHDRTFNQ TLRDNLQGII VNDCKQVDES MLPKRTWWNL
TKSVLAFHFL RHFPALVGWL PAHTPHLAQV PPPAQPEMET QDRVDPENSG VKP
