ID A0A157RGQ4_9BORD Unreviewed; 395 AA.
AC A0A157RGQ4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=ybhO {ECO:0000313|EMBL:SAI68623.1};
GN Synonyms=clsB {ECO:0000256|HAMAP-Rule:MF_01917};
GN ORFNames=SAMEA3906487_01356 {ECO:0000313|EMBL:SAI68623.1};
OS Bordetella trematum.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=123899 {ECO:0000313|EMBL:SAI68623.1, ECO:0000313|Proteomes:UP000076825};
RN [1] {ECO:0000313|EMBL:SAI68623.1, ECO:0000313|Proteomes:UP000076825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H044680328 {ECO:0000313|EMBL:SAI68623.1,
RC ECO:0000313|Proteomes:UP000076825};
RG Pathogen Informatics;
RL Submitted (APR-2016) 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}.
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DR EMBL; LT546645; SAI68623.1; -; Genomic_DNA.
DR RefSeq; WP_033535193.1; NZ_UFUJ01000001.1.
DR AlphaFoldDB; A0A157RGQ4; -.
DR STRING; 123899.SAMEA3906487_01356; -.
DR GeneID; 56591352; -.
DR KEGG; btrm:SAMEA390648701356; -.
DR PATRIC; fig|123899.6.peg.1334; -.
DR eggNOG; COG1502; Bacteria.
DR OrthoDB; 9762009at2; -.
DR Proteomes; UP000076825; Chromosome 1.
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:SF23; CARDIOLIPIN SYNTHASE B; 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:UP000076825};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01917, ECO:0000313|EMBL:SAI68623.1}.
FT DOMAIN 116..143
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 298..324
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT ACT_SITE 121
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 123
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 128
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 303
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 305
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 310
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
SQ SEQUENCE 395 AA; 44334 MW; 0481D6B6A1F82A44 CRC64;
MSATSGRLAW TDGNAIELLH NGAEFFPALC AAIEGAQHSI HLETYIFRLD RSGRVVLQAL
ERAARRGVRL RLVLDGFGSA ASAEMLVQRL RAAGGQCRIY RPEPSRLGWL KFSRRRLRRL
HRKVAVVDGR IAFVGGINIV DDHDDADPAR VAPRLDYAVR VEGPLVAQAR QAQASLWLRL
NWARHPGLWR HGLGRRHAAS GQGPLRAALV LRDNLRYRRT FERIYLAGID NAQREILIAN
AYFFPGRRFR EALLRAAARG LRVRLLLQGK PDYYLQYFAT RALYEPLLQA GIEIYEYMPS
GLHAKVAVID GIATVGSSNL DPFSLLLARE ANVLVDDAAF AQRLQTSLEQ VIAEGGQRVR
ASAYRQRGWW RRAGDALAYR ALRLAAALTG RRDDY
//
