CLSB_SALTY
ID CLSB_SALTY Reviewed; 413 AA.
AC Q8ZQP4;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=STM0812;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
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).
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; AE006468; AAL19749.1; -; Genomic_DNA.
DR RefSeq; NP_459790.1; NC_003197.2.
DR RefSeq; WP_000649648.1; NC_003197.2.
DR AlphaFoldDB; Q8ZQP4; -.
DR SMR; Q8ZQP4; -.
DR STRING; 99287.STM0812; -.
DR PaxDb; Q8ZQP4; -.
DR EnsemblBacteria; AAL19749; AAL19749; STM0812.
DR GeneID; 1252332; -.
DR KEGG; stm:STM0812; -.
DR PATRIC; fig|99287.12.peg.846; -.
DR HOGENOM; CLU_038053_0_0_6; -.
DR OMA; EYCQRPL; -.
DR PhylomeDB; Q8ZQP4; -.
DR BioCyc; SENT99287:STM0812-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008808; F:cardiolipin synthase activity; IBA:GO_Central.
DR GO; GO:0032049; P:cardiolipin biosynthetic process; IBA:GO_Central.
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_0000201287"
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; 47302 MW; 0710F4573A674072 CRC64;
MKCGWREGNQ IQLLENGDQF YPAVFEAIAQ AQQKIILETF ILFEDEVGKK LHTALLKAAQ
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 QDRVDPENTG VKP
