ID A0A0R2HB43_WEIVI Unreviewed; 484 AA.
AC A0A0R2HB43;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Cardiolipin synthase {ECO:0000256|HAMAP-Rule:MF_01916};
DE Short=CL synthase {ECO:0000256|HAMAP-Rule:MF_01916};
DE EC=2.7.8.- {ECO:0000256|HAMAP-Rule:MF_01916};
GN Name=cls {ECO:0000313|EMBL:QOD85665.1};
GN ORFNames=IE337_05540 {ECO:0000313|EMBL:QOD85665.1}, IV50_GL000397
GN {ECO:0000313|EMBL:KRN47127.1};
OS Weissella viridescens (Lactobacillus viridescens).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; Weissella.
OX NCBI_TaxID=1629 {ECO:0000313|EMBL:KRN47127.1, ECO:0000313|Proteomes:UP000051992};
RN [1] {ECO:0000313|EMBL:KRN47127.1, ECO:0000313|Proteomes:UP000051992}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20410 {ECO:0000313|EMBL:KRN47127.1,
RC ECO:0000313|Proteomes:UP000051992};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
RN [2] {ECO:0000313|EMBL:QOD85665.1, ECO:0000313|Proteomes:UP000516737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJ100 {ECO:0000313|EMBL:QOD85665.1,
RC ECO:0000313|Proteomes:UP000516737};
RA Lu X.;
RT "The complete genome sequence of Weissella viridescens NJ100 isolated from
RT low-temperature meat products.";
RL Submitted (SEP-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible phosphatidyl group transfer from one
CC phosphatidylglycerol molecule to another to form cardiolipin (CL)
CC (diphosphatidylglycerol) and glycerol. {ECO:0000256|HAMAP-
CC Rule:MF_01916}.
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:0000256|HAMAP-
CC Rule:MF_01916};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01916};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01916}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the phospholipase D family. Cardiolipin synthase
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01916}.
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DR EMBL; JQBM01000001; KRN47127.1; -; Genomic_DNA.
DR EMBL; CP061835; QOD85665.1; -; Genomic_DNA.
DR RefSeq; WP_057744289.1; NZ_JQBM01000001.1.
DR AlphaFoldDB; A0A0R2HB43; -.
DR KEGG; wvr:IE337_05540; -.
DR PATRIC; fig|1629.5.peg.401; -.
DR OrthoDB; 9762009at2; -.
DR Proteomes; UP000051992; Unassembled WGS sequence.
DR Proteomes; UP000516737; 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 CDD; cd09110; PLDc_CLS_1; 1.
DR CDD; cd09112; PLDc_CLS_2; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR HAMAP; MF_01916; Cardiolipin_synth_Cls; 1.
DR InterPro; IPR030874; Cardiolipin_synth_Firmi.
DR InterPro; IPR022924; Cardiolipin_synthase.
DR InterPro; IPR027379; CLS_N.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR NCBIfam; TIGR04265; bac_cardiolipin; 1.
DR PANTHER; PTHR21248; CARDIOLIPIN SYNTHASE; 1.
DR PANTHER; PTHR21248:SF22; PHOSPHOLIPASE D; 1.
DR Pfam; PF13091; PLDc_2; 2.
DR Pfam; PF13396; PLDc_N; 1.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR PROSITE; PS50035; PLD; 2.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_01916};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW Rule:MF_01916};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW Rule:MF_01916};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01916};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209,
KW ECO:0000256|HAMAP-Rule:MF_01916};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264, ECO:0000256|HAMAP-
KW Rule:MF_01916}; Reference proteome {ECO:0000313|Proteomes:UP000051992};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01916};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01916};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01916}.
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT TRANSMEM 35..56
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT DOMAIN 217..244
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 397..424
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT ACT_SITE 222
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 224
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 229
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 402
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 404
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 409
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
SQ SEQUENCE 484 AA; 55387 MW; 66F9D4CB6AFFB3FE CRC64;
MSSSIIFSII AIIFILNLIA AIITVFDEKR DIASIWAWLL VLLLFPVVGF FIYAFLGRKI
SHSKIFDLRT QEDLGIDQIA ENQRDLLAKN AEEDREKYSE QEPFFNLFLN SDEAVLTQKN
EVRLFNNGPE KFKALFEDIR NAKNHINVEY FSIFDDELGN QLVDLLTEKA HEGVKVRVLF
DQFGSHGRNK KLYERLRAAG GQDMAFLESP WPITFRANFR LHRKLVVIDG KIGYIGGLNV
GDEYVGKSKK FGNWRDTHTR IVGDAVLALQ GRFFMDWNAT AKKENKLQFS KDYFPNDTEG
NGNTAVQIVT SGPDQDTQQI KQGYMRQIAS ARESITIQTP YFIPDQGMMD LLTVAAMSGV
KVRLMIPCMP DHPFVYRATE YYAKELLDAG GEVYTYDNGF IHAKVVTIDG KVSSVGSANM
DMRSFGLNFE GNAFMYDEDI AKQLEDFFEQ DIKASTHLNE QYFENQSKWL KFKQKFSRLL
SPIL
//
