ID G4F9C1_9GAMM Unreviewed; 401 AA.
AC G4F9C1;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=HAL1_15006 {ECO:0000313|EMBL:EHA14732.1};
OS Halomonas sp. HAL1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=550984 {ECO:0000313|EMBL:EHA14732.1, ECO:0000313|Proteomes:UP000005692};
RN [1] {ECO:0000313|EMBL:EHA14732.1, ECO:0000313|Proteomes:UP000005692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain {ECO:0000313|Proteomes:UP000005692};
RX PubMed=22156396; DOI=10.1128/JB.06359-11;
RA Lin Y., Fan H., Hao X., Johnstone L., Hu Y., Wei G., Alwathnani H.A.,
RA Wang G., Rensing C.;
RT "Draft Genome Sequence of Halomonas sp. Strain HAL1, a Moderately
RT Halophilic Arsenite-Oxidizing Bacterium Isolated from Gold-Mine Soil.";
RL J. Bacteriol. 194:199-200(2012).
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:EHA14732.1}.
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DR EMBL; AGIB01000073; EHA14732.1; -; Genomic_DNA.
DR AlphaFoldDB; G4F9C1; -.
DR PATRIC; fig|550984.5.peg.2895; -.
DR Proteomes; UP000005692; 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; 3.
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 PIRSF; PIRSF000850; Phospholipase_D_PSS; 3.
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 110..137
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 284..311
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT ACT_SITE 115
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 117
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 122
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 289
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 291
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 296
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
SQ SEQUENCE 401 AA; 45919 MW; AD363742E6F0D9BC CRC64;
MLVNFQWTES NEAELLINGS QYFNSVFDCI RSAREEVLIE TFIIFNDEVG RELKEALLDA
AARQVRIDVT VDGYGTADLD NDYITELTDA GIHLHVYDPK PRLFGMRTNL FRRLHRKIVV
VDGDVAFIGG INFGADHLPD KYAMGKQDYG LRVRGPIVKD IRDAAGALLV EHQAVQELPQ
IRALPPPTGS AAIRLAIRDN SLHRNDIEEH YLQAFRSAQS HLVIANAYFF PSYRLFHELR
NAARRGVNVT LILQGRPDMP WARMFSSSLY SYMLQQGISI FEYTEHPLHG KIAIVDHEWS
TVGSSNLDPL SLSLNLEANL FVRDARLNQQ IHQHLSELIE SSCKRITTEA AEKGRWWRAP
LMFASFHFLR HFPRRMGWLP AHVARMETLA PRSRKHKRAQ E
//
