ID A0A106BWG6_THIDE Unreviewed; 396 AA.
AC A0A106BWG6;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=ABW22_00645 {ECO:0000313|EMBL:KVW99703.1};
OS Thiobacillus denitrificans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Thiobacillaceae; Thiobacillus.
OX NCBI_TaxID=36861 {ECO:0000313|EMBL:KVW99703.1, ECO:0000313|Proteomes:UP000064243};
RN [1] {ECO:0000313|EMBL:KVW99703.1, ECO:0000313|Proteomes:UP000064243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RG {ECO:0000313|EMBL:KVW99703.1,
RC ECO:0000313|Proteomes:UP000064243};
RX PubMed=26712544;
RA Harrold Z.R., Skidmore M.L., Hamilton T.L., Desch L., Amada K.,
RA van Gelder W., Glover K., Roden E.E., Boyd E.S.;
RT "Aerobic and Anaerobic Thiosulfate Oxidation by a Cold-Adapted, Subglacial
RT Chemoautotroph.";
RL Appl. Environ. Microbiol. 82:1486-1495(2015).
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:KVW99703.1}.
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DR EMBL; LDUG01000002; KVW99703.1; -; Genomic_DNA.
DR RefSeq; WP_059750886.1; NZ_LDUG01000002.1.
DR AlphaFoldDB; A0A106BWG6; -.
DR STRING; 1123392.GCA_000376425_03468; -.
DR PATRIC; fig|36861.3.peg.1164; -.
DR OrthoDB; 9762009at2; -.
DR Proteomes; UP000064243; 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: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:UP000064243};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01917}.
FT DOMAIN 119..146
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 299..326
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT ACT_SITE 124
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 126
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 131
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 304
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 306
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 311
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
SQ SEQUENCE 396 AA; 44010 MW; 18BB3BCFDA642E8B CRC64;
MKTPLRKLFF RGAGLVSGNQ LRLLQSGVEF FPALIAAIDV AHSEIHLETY IFNVDPSTEA
VRDALTRAAL RGVRVRLLID GVGSRELPAA WLDALRTAGV SVLRYRPLAG RGWRSNPKSL
RRLHRKLAVI DARIALVGGM NLIDDFEPAH FDVPRLDFSV EVQGPLLAGI HQSARHLWRL
VALTQLRAGE SRPPLIQPSW PTDGHVRAAF VVRDNFAHRR DIERAYLAAL ALAHDEIILA
NAYFLPGYRF RRLLKNAAAR GVRVHLLVQG HTDHPFFLAA ARALYHDLLA AGVSIHEYQA
SELHAKVAVV DSHWATVGSS NIDPFSLLLA REANIVVDDA AFAHDLRQRL HHAISQSVPL
DAAGWQRRAW PHRMLSWLAY GGVRLMVGLA GVGRWV
//
