ID A0A2P8VQ87_9ENTR Unreviewed; 414 AA.
AC A0A2P8VQ87;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=C7G83_02115 {ECO:0000313|EMBL:PSN09560.1};
OS Siccibacter turicensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Siccibacter.
OX NCBI_TaxID=357233 {ECO:0000313|EMBL:PSN09560.1, ECO:0000313|Proteomes:UP000240212};
RN [1] {ECO:0000313|EMBL:PSN09560.1, ECO:0000313|Proteomes:UP000240212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6100069499-17 {ECO:0000313|EMBL:PSN09560.1,
RC ECO:0000313|Proteomes:UP000240212};
RA Lepuschitz S., Pekard-Amenitsch S., Haunold R., Schill S., Mach R.,
RA Allerberger F., Ruppitsch W., Forsythe S.J.;
RT "Draft genome sequence of the first documented clinical Siccibacter
RT turicensis isolate in Austria.";
RL Submitted (MAR-2018) 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}.
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:PSN09560.1}.
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DR EMBL; PYEP01000001; PSN09560.1; -; Genomic_DNA.
DR RefSeq; WP_024548266.1; NZ_RYYT01000002.1.
DR AlphaFoldDB; A0A2P8VQ87; -.
DR STRING; 1388748.GCA_000463155_01516; -.
DR OrthoDB; 9762009at2; -.
DR Proteomes; UP000240212; 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 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 393..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..414
FT /note="Basic and acidic residues"
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; 47418 MW; 373AE0D72C985ED2 CRC64;
MKPAWRDGNR IELLENGDEF FPAVFEAIGE AKDKVILETF IWFEDDVGKA LHRAILDAAQ
RGVSVEVLLD GYGSPDLSDE FVTQLTAAGV KFRYYDPRPP LLGMRTNVFR RMHRKIVVID
GELAFVGGIN YSAEHMSDYG PEAKQDYAVR VQGPVVQDIY AFVLSNLPGH EEARRWWSRR
RHQAQDNSTP GEAQALFVWR DNGEHRDDIE RYYLKMLANA KQEVIIANAY FFPGYRLLHA
MRNAARRGVR VKLVVQGEPD MPIVKVGARL LYNYLVKGGV EVYEYLRRPL HGKVALMDDH
WATVGSSNLD PLSLSLNLEA NLIIHDRAFN QTLRDNLTRL IEEDCQQVDE TLMPKRTWWN
LGKSVIVFHF LRHFPALVGW LPAHTPRLSL VEPPVQPEME TQDRVETDNP GAKF
//
