ID A0A1S8FGM6_9BURK Unreviewed; 419 AA.
AC A0A1S8FGM6;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Cardiolipin synthase B {ECO:0000256|HAMAP-Rule:MF_01917};
DE Short=CL synthase {ECO:0000256|HAMAP-Rule:MF_01917};
DE EC=2.7.8.- {ECO:0000256|HAMAP-Rule:MF_01917};
GN Name=clsB {ECO:0000256|HAMAP-Rule:MF_01917};
GN ORFNames=B0B52_12525 {ECO:0000313|EMBL:OOG41158.1};
OS Polaromonas sp. A23.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=1944133 {ECO:0000313|EMBL:OOG41158.1, ECO:0000313|Proteomes:UP000218978};
RN [1] {ECO:0000313|EMBL:OOG41158.1, ECO:0000313|Proteomes:UP000218978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A23 {ECO:0000313|EMBL:OOG41158.1,
RC ECO:0000313|Proteomes:UP000218978};
RA Lycus P., Bothun K.L., Bergaust L., Shapleigh J.P., Bakken L.R.,
RA Frostegard A.;
RT "Phenotypic and genotypic richness of denitrifiers revealed by a novel
RT isolation strategy.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the phosphatidyl group transfer from one
CC phosphatidylglycerol molecule to another to form cardiolipin (CL)
CC (diphosphatidylglycerol) and glycerol. {ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_01917};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01917};
CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01917}.
CC -!- SIMILARITY: Belongs to the phospholipase D family. Cardiolipin synthase
CC subfamily. ClsB sub-subfamily. {ECO:0000256|HAMAP-Rule:MF_01917}.
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:OOG41158.1}.
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DR EMBL; MUNO01000022; OOG41158.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S8FGM6; -.
DR STRING; 1944133.B0B52_12525; -.
DR OrthoDB; 9762009at2; -.
DR Proteomes; UP000218978; 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; cd09159; PLDc_ybhO_like_2; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
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 PANTHER; PTHR21248; CARDIOLIPIN SYNTHASE; 1.
DR PANTHER; PTHR21248:SF22; PHOSPHOLIPASE D; 1.
DR Pfam; PF13091; PLDc_2; 2.
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|HAMAP-Rule:MF_01917};
KW Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01917};
KW Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01917};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_01917};
KW Phospholipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01917};
KW Phospholipid metabolism {ECO:0000256|HAMAP-Rule:MF_01917};
KW Reference proteome {ECO:0000313|Proteomes:UP000218978};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01917}.
FT DOMAIN 112..139
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 323..350
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT ACT_SITE 117
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 119
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 124
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 328
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 330
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 335
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
SQ SEQUENCE 419 AA; 46263 MW; 26AF54BBD0562D1D CRC64;
MPSLTTQHAL QLLQGGQALF PAMVKALDEA TAWVQLETYI FDFHGRGEEL AQALLRAARR
GVLVQVLVDG IGTNRPSAEW QGRFAEAGVQ WQEYAPLGRG RFAVLGLLVP ERWRRLHRKL
CVVDELTVFC GGINILDDFY DPNHGDLTAP RFDFAVAVTG PLAAEASDAM ALLWWRVQAG
YSARQRHLSA AWEAVKAAGY GGRSGTDRKG RALLSLLGRT TDATASVSGA KAALVLRDNL
FHRSSIERAY RRAIGQAHEE IIIANAYFVP GGKLRRALVQ AARRGVRVTL LLQGRYEYFM
QYHAARPVYG ALLAAGIEIH EYGAGFLHSK VAVIDGHWAT VGSSNLDPLS LLLAREANVV
VDDRAFALDL HQRLLRAMAG EGRRLDPAAY SRRPLRQRVL DYMAYALMRL ALLVAGQRY
//
