ID A0A1G5SAC3_9PROT Unreviewed; 389 AA.
AC A0A1G5SAC3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 13.
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:SCZ84155.1};
GN Synonyms=clsB {ECO:0000256|HAMAP-Rule:MF_01917};
GN ORFNames=NSMM_1080005 {ECO:0000313|EMBL:SCZ84155.1};
OS Nitrosomonas mobilis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=51642 {ECO:0000313|EMBL:SCZ84155.1, ECO:0000313|Proteomes:UP000198729};
RN [1] {ECO:0000313|EMBL:SCZ84155.1, ECO:0000313|Proteomes:UP000198729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1 {ECO:0000313|EMBL:SCZ84155.1};
RA de Groot N.N.;
RL Submitted (OCT-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; FMWO01000011; SCZ84155.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5SAC3; -.
DR STRING; 51642.NSMM_1080005; -.
DR OrthoDB; 9762009at2; -.
DR Proteomes; UP000198729; 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; 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:UP000198729};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01917, ECO:0000313|EMBL:SCZ84155.1}.
FT DOMAIN 109..136
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 289..316
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT ACT_SITE 114
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 116
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 121
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 294
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 296
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 301
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
SQ SEQUENCE 389 AA; 44597 MW; CBA41BA0A3FCD56D CRC64;
MNVPEFVEGN QLRLLHTGTE YFLALEKAID QATQEIFLET YIFQDDCAGQ RIAAALVRAA
GRGVAVHVLI DGFGSQYYPE ENIRKLLEKS VQLLIYRQEI FSLRLKRQRL RRLHRKLAIM
DASIAFVGGI NIIDDFSGPD ITSPQFDYAV EIRGPLLQFI HAAARHLWTL VAWAHFKKRW
TNYAPVIGQQ RPAGRQRAAF VIRDNLRNRR NIEHCYLQAI ESANREILIA NAYFLPGINF
RHALIEAARR GVRVVLLLQG KTEHLVQHLA TRALYGNLLA AGIHIYEYRH GYLHAKVAVI
DQCWATVGSS NIDPLSLLLA REANVIIDDH EFALQLRDGL LQGMKKSYPV LRYSWKKRSG
LARLINWLCY YSVRIVQGML GYAHQEYKL
//
