ID A0A0G3BFS3_9BURK Unreviewed; 425 AA.
AC A0A0G3BFS3;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
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:AKJ28197.1};
GN Synonyms=clsB {ECO:0000256|HAMAP-Rule:MF_01917};
GN ORFNames=AAW51_1506 {ECO:0000313|EMBL:AKJ28197.1};
OS Caldimonas brevitalea.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Caldimonas.
OX NCBI_TaxID=413882 {ECO:0000313|EMBL:AKJ28197.1, ECO:0000313|Proteomes:UP000035352};
RN [1] {ECO:0000313|EMBL:AKJ28197.1, ECO:0000313|Proteomes:UP000035352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7029 {ECO:0000313|EMBL:AKJ28197.1,
RC ECO:0000313|Proteomes:UP000035352};
RA Tang B., Yu Y.;
RL Submitted (MAY-2015) 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; CP011371; AKJ28197.1; -; Genomic_DNA.
DR RefSeq; WP_047194107.1; NZ_CP011371.1.
DR AlphaFoldDB; A0A0G3BFS3; -.
DR STRING; 413882.AAW51_1506; -.
DR KEGG; pbh:AAW51_1506; -.
DR PATRIC; fig|413882.6.peg.1581; -.
DR OrthoDB; 9762009at2; -.
DR Proteomes; UP000035352; Chromosome.
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 PIRSF; PIRSF000850; Phospholipase_D_PSS; 3.
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:UP000035352};
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 290..317
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 394..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..410
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 295
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 297
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 302
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
SQ SEQUENCE 425 AA; 48025 MW; 0BD4C2E3D807D236 CRC64;
MTERHLPDWR DGNRFELLEN GEEFFPRVFE AIRSAHREVL VETFILFDDK VGQQLREELI
AAASRGVQVD LTVDGYGSPD LSVEFVSGMT AAGVRFHVFD PKPKLLGLRT NVFRRLHRKL
VVVDGQLAFV GGINFSVEHL WEYGPAAKQD YAVAVVGPVV ADIHRFAVDA IGERTASRRR
RAKAPAGVRQ GADVGPGRAT FVTRDNREHH TDIEQHYLFA IRSARRRVWI ANAYFFPGYR
LLRELRRAAR RGVEVALILQ GEPDMPIAKN AARTLYDGLL RDGVRIYEYC QRPLHGKVAV
VDDEWATVGS SNLDPLSLSL NLEANLVIRD AAFNAELAGR LQRLIDHHCQ LISVHDPAFE
VKRWHQWAGF LVYHFLRRFP AWSGWLPAHK PKLELVTPPP HQPPADPPVR NAHQQPATKG
AGYLP
//
