ID A0A3M7TWN9_9BACI Unreviewed; 503 AA.
AC A0A3M7TWN9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
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:RNA69893.1};
GN ORFNames=EBO34_08160 {ECO:0000313|EMBL:RNA69893.1};
OS Alteribacter keqinensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alteribacter.
OX NCBI_TaxID=2483800 {ECO:0000313|EMBL:RNA69893.1, ECO:0000313|Proteomes:UP000278746};
RN [1] {ECO:0000313|EMBL:RNA69893.1, ECO:0000313|Proteomes:UP000278746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KQ-3 {ECO:0000313|EMBL:RNA69893.1,
RC ECO:0000313|Proteomes:UP000278746};
RA Wang H.;
RT "Bacillus Keqinensis sp. nov., a moderately halophilic bacterium isolated
RT from a saline-alkaline lake.";
RL Submitted (OCT-2018) 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}.
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:RNA69893.1}.
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DR EMBL; RHIB01000001; RNA69893.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M7TWN9; -.
DR OrthoDB; 9762009at2; -.
DR Proteomes; UP000278746; 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:SF20; CARDIOLIPIN SYNTHASE YWIE-RELATED; 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:UP000278746};
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 7..25
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT TRANSMEM 31..50
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT DOMAIN 238..265
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 416..443
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT ACT_SITE 243
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 245
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 250
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 421
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 423
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 428
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
SQ SEQUENCE 503 AA; 57767 MW; 6E23D57FB113B178 CRC64;
MLKRLQIIVF LAIIIAGLLI TGQLWEGWLF GWASIFFSLT AFFIAVVIFL ENRNPTKTLA
WLMVLGIFPL LGFIFYLMFG QNHRKRKSFT KKAIMDEQAF SKIEGNRPLD ESQLGLMLEN
QQKLFRLAHR LANNPISFQT DTRVLTDGKE TFYHIKRALQ SATDHIHLEY YIVRDDELGC
EIKDILIAKA KEGVEVRFLF DAVGCWKLSK AYVSELRDAG VQMVAFSPVR LPFFTNKINY
RNHRKIIVVD TSYAFIGGLN IGDEYLGKSS YFGHWRDTHL LVRGEAVRSL QLIFLRDWYY
ATGEAALKPG YLSPTLPDGE HEGGVQMIAS GPDSRWEVIK KLFFTMITSA KRSIWIASPY
FIPDEDMLSA IKIAALGGID VRILVPSKPD KKIVFHASRS YFPELLEAGV KIYEYNRGFM
HSKIIIVDNE IASIGTANMD MRSFHLNFEV NAFLYRTRSV ENLASDFVYD MEHSTIIRQE
AFVKRSFYYK LVESTSRLMS PLL
//
