ID W0HT21_9GAMM Unreviewed; 414 AA.
AC W0HT21;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
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:AHF75672.1};
GN Synonyms=clsB {ECO:0000256|HAMAP-Rule:MF_01917};
GN ORFNames=Sant_0576 {ECO:0000313|EMBL:AHF75672.1};
OS Sodalis praecaptivus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Bruguierivoracaceae; Sodalis.
OX NCBI_TaxID=1239307 {ECO:0000313|EMBL:AHF75672.1, ECO:0000313|Proteomes:UP000019028};
RN [1] {ECO:0000313|EMBL:AHF75672.1, ECO:0000313|Proteomes:UP000019028}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS1 {ECO:0000313|EMBL:AHF75672.1,
RC ECO:0000313|Proteomes:UP000019028};
RX PubMed=24407854; DOI=10.1093/gbe/evt210;
RA Oakeson K.F., Gil R., Clayton A.L., Dunn D.M., von Niederhausern A.C.,
RA Hamil C., Aoyagi A., Duval B., Baca A., Silva F.J., Vallier A.,
RA Jackson D.G., Latorre A., Weiss R.B., Heddi A., Moya A., Dale C.;
RT "Genome degeneration and adaptation in a nascent stage of symbiosis.";
RL Genome Biol. Evol. 6:76-93(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; CP006569; AHF75672.1; -; Genomic_DNA.
DR RefSeq; WP_025420803.1; NZ_CP006569.1.
DR AlphaFoldDB; W0HT21; -.
DR KEGG; sod:Sant_0576; -.
DR PATRIC; fig|1239307.3.peg.617; -.
DR HOGENOM; CLU_038053_0_0_6; -.
DR OrthoDB; 9762009at2; -.
DR Proteomes; UP000019028; 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 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:UP000019028};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01917}.
FT DOMAIN 108..135
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 286..313
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 394..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 113
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 115
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 120
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 291
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 293
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 298
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
SQ SEQUENCE 414 AA; 47826 MW; 702A6F9415749969 CRC64;
MNMEWREGNR IKLLENGEAF FPRLHERIHA AEKEVLLETF ILFEDKVGRE LQQVLIAAAQ
RGVRVELTVD GYGSPDLSDD FVAAMTGAGV RFRYYDPRPA FMGMRTNLFR RLHRKIVVVD
AHLAFVGGIN FSHEHLSDYG PQAKQDYAVE IEGPVVEDIH RYCLRALYKR DEQRNWWGRR
SRPPAPNRRP GDAQALFVYR DNDEHATDIE QHYLEMLRSA KRDVIIANAY FFPGYRLLKE
MRNAARRGVN VVLIVQGEPD MPIVQVGARM LYHYLVPEGV KIYEYCRRPL HAKVALKDDA
WATVGSSNLD PLSLALNLEA NVIIHDRAFN RELRDNLDRL IANDCQWVDE SKVPRQTYWH
LAKSVLVFHF LRHFPAWVGW LPAHTPKLAL VPAPVQPEME TQDRTDTENG SVKP
//
