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Database: UniProt
Entry: A0A497XJ17_9PROT
LinkDB: A0A497XJ17_9PROT
Original site: A0A497XJ17_9PROT 
ID   A0A497XJ17_9PROT        Unreviewed;       392 AA.
AC   A0A497XJ17;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   24-JAN-2024, entry version 10.
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=DFR35_0475 {ECO:0000313|EMBL:RLJ67922.1};
OS   Sulfurisoma sediminicola.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Sterolibacteriaceae; Sulfurisoma.
OX   NCBI_TaxID=1381557 {ECO:0000313|EMBL:RLJ67922.1, ECO:0000313|Proteomes:UP000268908};
RN   [1] {ECO:0000313|EMBL:RLJ67922.1, ECO:0000313|Proteomes:UP000268908}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26916 {ECO:0000313|EMBL:RLJ67922.1,
RC   ECO:0000313|Proteomes:UP000268908};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (OCT-2018) 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:RLJ67922.1}.
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DR   EMBL; RCCI01000004; RLJ67922.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A497XJ17; -.
DR   OrthoDB; 9762009at2; -.
DR   Proteomes; UP000268908; 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:UP000268908};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01917}.
FT   DOMAIN          108..135
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          291..318
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   ACT_SITE        113
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT   ACT_SITE        115
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT   ACT_SITE        120
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT   ACT_SITE        296
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT   ACT_SITE        298
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT   ACT_SITE        303
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
SQ   SEQUENCE   392 AA;  43353 MW;  461FED7E0B791B00 CRC64;
     MKPRFAAGNR VELLETGAEY FPALIAAIDA AATEVHLQTY IFANDATGRA VSAALAQASR
     RGVAVRVLVD GFGAREFPTA FGAELERAGV EVLVYRAEIA PLRLRRHRLR RLHRKVAVID
     GRVGFVGGIN IIDDWDMGTT PEQIPPRYDY AVRIEGPLLA AIHASTRQIW QLVRWARLRR
     RLLDPPHRAP DDTPRGGIRA AFVVRDNLRH RRDIEEAYLD AIAGARQEVL LASAYFLPGR
     RFRHALAGAA KRGVQVTVLL QGRVEYRLLH HATQALYGAL FGSGIRIFEY HKSFLHAKVA
     VIDCCWSTVG SSNIDPFSLL MAREANVVVA DAAFGAALRA SLQGAMDAGA REVRHEDWRA
     APLPMRVARW LAYGVVRLAM GIVGYGRKDY SG
//
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