ID E0X710_PSEPU Unreviewed; 400 AA.
AC E0X710;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 30.
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};
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303 {ECO:0000313|EMBL:ADI95344.1};
RN [1] {ECO:0000313|EMBL:ADI95344.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DOT-T1E {ECO:0000313|EMBL:ADI95344.1};
RA Daniels C., Godoy P., Duque E., Molina-Henares M.A., de la Torre J.,
RA Del Arco J.M., Herrera C., Segura A., Guazzaroni M.E., Ferrer M.,
RA Ramos J.L.;
RT "Global regulation of food supply by Pseudomonas putida DOT-T1E.";
RL Submitted (AUG-2009) 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}.
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DR EMBL; GQ848197; ADI95344.1; -; Genomic_DNA.
DR AlphaFoldDB; E0X710; -.
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 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 108..135
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 280..307
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
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 285
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 287
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 292
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
SQ SEQUENCE 400 AA; 45424 MW; FDE99B5197507883 CRC64;
MNRPWVDGNS VQLLINGEQY YPRVFEAMAQ AREEILLETF IIFDDKVGKQ LQQVLIEAAR
RGVRVEVAAD GYGTAELPAE FISAMTDAGV SFHAFDPQPL LLGMRTNLFR RLHRKIVVVD
GERAFIGGIN YSADHLGDFG AMAKQDYAVE VTGPVVAQVH AASKRLMSPV LQPPSAVRPV
TEPAGSSSAV LIERDNGMRS TDIEAHYLQA FRKARQRIVV ANAYFFPGYR LMRELRNAAR
RGVEVRLILQ GQPDMRWVRA LSRLLYNYLL RDGVKIHEYC QRPLHGKVAL VDDQWATVGS
SNLDPLSLSF NLEANLFIRD RAFNQQLHQH LQALASEQCK PVTLERMIRG YWWRAPLIFV
CFHVIRHFPR IAGWFPAHRQ RLRSVQPEAE PHGNLHEGNS
//
