ID A0A0R2NHL0_9LACO Unreviewed; 475 AA.
AC A0A0R2NHL0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
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 ORFNames=IV88_GL000323 {ECO:0000313|EMBL:KRO25287.1};
OS Pediococcus argentinicus.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Pediococcus.
OX NCBI_TaxID=480391 {ECO:0000313|EMBL:KRO25287.1, ECO:0000313|Proteomes:UP000051249};
RN [1] {ECO:0000313|EMBL:KRO25287.1, ECO:0000313|Proteomes:UP000051249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23026 {ECO:0000313|EMBL:KRO25287.1,
RC ECO:0000313|Proteomes:UP000051249};
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).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRO25287.1}.
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DR EMBL; JQCQ01000013; KRO25287.1; -; Genomic_DNA.
DR RefSeq; WP_057799206.1; NZ_JQCQ01000013.1.
DR AlphaFoldDB; A0A0R2NHL0; -.
DR PATRIC; fig|480391.4.peg.327; -.
DR OrthoDB; 9762009at2; -.
DR Proteomes; UP000051249; Unassembled WGS sequence.
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:UP000051249};
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..22
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT TRANSMEM 29..51
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT DOMAIN 210..237
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 388..415
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT ACT_SITE 215
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 217
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 222
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 393
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 395
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 400
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
SQ SEQUENCE 475 AA; 54636 MW; E1652583CD46564C CRC64;
MIWIEIGLYL LNALIAITIA LFERRDIAAA WAWMLVMFLL PGVGLLAYMF LGRKLSSNQI
FDIRAQQNLG VSEMARYQKE SSANHIQLES PMETELVNLF LNTDDAILTH QNEVMLLNDG
KRKFKQLFRD LKHARYNINI EYFTIYNDDL GQQLRDILVQ KAKAGVRIKV MYDLFGSKGS
KTAMFKELIE NGGEVIPFMR PRFSYLNFRI NFRNHRKIVV IDGSIGYIGG FNVGDQYVGQ
NSRFGYWRDT HLRITGSAVL QLQSRFFMDW NASNKKNTER IDISYFPQNE VHGNVPIQIV
SSGPESEIQK IKQGYIKMIA AAQSSIKIET PYFIPDDALM EILLIAIKTG VHVTLVIPNQ
PDHFFVYRAT EYYAQQLVAA GANVYMYQKG FMHVKTIIVD EKVVSVGSAN LDIRSFKLNF
EANAFIYNQQ IAQQVGQDIK QDINDSELLT EHYFKNQSNW TKIKQQFSRL LSPIL
//
