ID A2SEP5_METPP Unreviewed; 437 AA.
AC A2SEP5;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 87.
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 OrderedLocusNames=Mpe_A1073 {ECO:0000313|EMBL:ABM94034.1};
OS Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Methylibium.
OX NCBI_TaxID=420662 {ECO:0000313|EMBL:ABM94034.1, ECO:0000313|Proteomes:UP000000366};
RN [1] {ECO:0000313|EMBL:ABM94034.1, ECO:0000313|Proteomes:UP000000366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1232 / LMG 22953 / PM1
RC {ECO:0000313|Proteomes:UP000000366};
RX PubMed=17158667; DOI=10.1128/JB.01259-06;
RA Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA Hristova K.R.;
RT "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT proteobacterium Methylibium petroleiphilum PM1.";
RL J. Bacteriol. 189:1931-1945(2007).
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; CP000555; ABM94034.1; -; Genomic_DNA.
DR RefSeq; WP_011828671.1; NC_008825.1.
DR AlphaFoldDB; A2SEP5; -.
DR STRING; 420662.Mpe_A1073; -.
DR KEGG; mpt:Mpe_A1073; -.
DR eggNOG; COG1502; Bacteria.
DR HOGENOM; CLU_038053_0_0_4; -.
DR Proteomes; UP000000366; 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; 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:UP000000366};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01917, ECO:0000313|EMBL:ABM94034.1}.
FT DOMAIN 133..160
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 341..368
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT ACT_SITE 138
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 140
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 145
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 346
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 348
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 353
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
SQ SEQUENCE 437 AA; 48343 MW; 567801DC12ADDB7D CRC64;
MTAPAGAPPP DDPVLSEALA WYAHARAVFS GGNEVQLLRG GDALFPAMIE SIGHATHEVW
LATYIYGDDV AAQAVSAALV AAARRGVRVR VVVDGFGSLH ALAALRERLE PAGVALAVFR
PTQRWWNWLQ PGQLRRLHQK LCVVDGQVGF VGGINVLDDR HDLNHGWGDT PRLDYAVRVR
GAVVGPVEQT ARAMWTRAAF GRDWRDEVRQ IARSSQPMAR ARRLLRRLRI AVRRGSPGGF
GAGALQPVRV AFVVRDNLSQ RRSIERSYID ALRRAQQRID IVSAYFYPGF EFRRALLAAA
RRGVRVRLLL QGKADYRFAA LAAQALYDEL LAHGVAVFEY TPAFLHAKVA LVDQRWATVG
SSNIDPLSLL VNLEANVIVD DRGFAATLSR ELDRDFAVSR EITAPVPVAG WRRWLRRGFV
AWVARLYLRA AGAGGRY
//
