ID W0SAW7_9PROT Unreviewed; 397 AA.
AC W0SAW7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=SUTH_00060 {ECO:0000313|EMBL:BAO27880.1};
OS Sulfuritalea hydrogenivorans sk43H.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Sterolibacteriaceae; Sulfuritalea.
OX NCBI_TaxID=1223802 {ECO:0000313|EMBL:BAO27880.1, ECO:0000313|Proteomes:UP000031637};
RN [1] {ECO:0000313|EMBL:BAO27880.1, ECO:0000313|Proteomes:UP000031637}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM22779 {ECO:0000313|EMBL:BAO27880.1};
RX PubMed=25017294; DOI=10.1016/j.syapm.2014.05.010;
RA Watanabe T., Kojima H., Fukui M.;
RT "Complete genomes of freshwater sulfur oxidizers Sulfuricella denitrificans
RT skB26 and Sulfuritalea hydrogenivorans sk43H: genetic insights into the
RT sulfur oxidation pathway of betaproteobacteria.";
RL Syst. Appl. Microbiol. 37:387-395(2014).
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; AP012547; BAO27880.1; -; Genomic_DNA.
DR RefSeq; WP_052472979.1; NZ_AP012547.1.
DR AlphaFoldDB; W0SAW7; -.
DR STRING; 1223802.SUTH_00060; -.
DR KEGG; shd:SUTH_00060; -.
DR HOGENOM; CLU_038053_0_0_4; -.
DR OrthoDB; 9762009at2; -.
DR Proteomes; UP000031637; 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: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:UP000031637};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01917}.
FT DOMAIN 116..143
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 296..323
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 301
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 303
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 308
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
SQ SEQUENCE 397 AA; 43664 MW; 66E7065E8952D57C CRC64;
MSADRGDAAS HDFLAGNRLS LLNSGGEYFP ALIAQIDAAV HEVHLETYIF ADDATGRLVA
AALNRAAQRG VAVRVLVDGF GAREFAAGLG VELEAGGVEV MTYRPEVGNT RFRRHRLRRL
HRKLSVFDGR VAFVGGINVI DDFDDGKAES ARFDYAVRIE GPLVPRIHAA MRHVWRLVRW
ARLGRRPPPP AALPVVPAAS GTTKAALLVR DNLRHRRDIE NAYLAAIHSA REEIVISNAY
FLPGRRFRNA LLAAAKRGVS VKLLLQGRVE HVLQHYATQS LYDRMLAAGV RVFEYEKAFL
HAKVAVIDGD WATVGSSNID PFSLLLAREA NVVVRDAEFA GQLRASLLTA IEGVAIEIRA
EDQRSRSWLV RLASAAAYGL VRFMIGVTRY GGKQYAD
//
