ID C5D1W9_VARPS Unreviewed; 413 AA.
AC C5D1W9;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
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=Vapar_6327 {ECO:0000313|EMBL:ACS22889.1};
OS Variovorax paradoxus (strain S110).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=543728 {ECO:0000313|EMBL:ACS22889.1};
RN [1] {ECO:0000313|EMBL:ACS22889.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S110 {ECO:0000313|EMBL:ACS22889.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Orwin P.,
RA Leadbetter J.R., Spain J.C., Han J.I.;
RT "Complete sequence of chromosome 2 of Variovorax paradoxus S110.";
RL Submitted (JUN-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; CP001636; ACS22889.1; -; Genomic_DNA.
DR AlphaFoldDB; C5D1W9; -.
DR STRING; 543728.Vapar_6327; -.
DR KEGG; vap:Vapar_6327; -.
DR eggNOG; COG1502; Bacteria.
DR HOGENOM; CLU_038053_0_0_4; -.
DR OrthoDB; 9762009at2; -.
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 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 117..144
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 307..334
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 181..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 122
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 124
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 129
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 312
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 314
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 319
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
SQ SEQUENCE 413 AA; 46677 MW; DA6EF00420242C71 CRC64;
MKNSPTRGLA RARWVPGNRV SLLENGEEFF PRVFEAVRRA QREVLIETFI LYEDKVGTQL
HACLCEAARR GVRVDLLVDG FGSPDLSEAF IQEMAAAGVR LRVFDPGHSI LGQRLNLLRR
MHRKIVVVDD ACAFVGGINF SADQLLDFGA TAKQDYAVEL NGPIVQLIHR FAARAVAADK
KKAKQGARSH RPAPPERQQE GSGHATGHAR AGEAEVCLVT RDNWRHTNDI ERHYRVAIRS
ARQRVVIANA YFFPGYRLIQ DMRNAARRGV DVRLILQGEP DIPIVRIAAR MLYHHLLMAG
VSIFEYCERP MHAKVALTDD CWSTVGSSNL DPLSLALNLE ANVVVHDPAF NRALSERLEH
MNRNCKRIGA ADLDKWSSWR LVRSFVVFHL LRWYPSWIAW LPRHAPRVTA LGR
//
