ID A0A0Q6XES4_9BURK Unreviewed; 413 AA.
AC A0A0Q6XES4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=ASC87_02205 {ECO:0000313|EMBL:KQV99535.1};
OS Rhizobacter sp. Root1221.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Rhizobacter.
OX NCBI_TaxID=1736433 {ECO:0000313|EMBL:KQV99535.1, ECO:0000313|Proteomes:UP000051465};
RN [1] {ECO:0000313|EMBL:KQV99535.1, ECO:0000313|Proteomes:UP000051465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1221 {ECO:0000313|EMBL:KQV99535.1,
RC ECO:0000313|Proteomes:UP000051465};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQV99535.1, ECO:0000313|Proteomes:UP000051465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1221 {ECO:0000313|EMBL:KQV99535.1,
RC ECO:0000313|Proteomes:UP000051465};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQV99535.1}.
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DR EMBL; LMDI01000012; KQV99535.1; -; Genomic_DNA.
DR RefSeq; WP_056660338.1; NZ_LMDI01000012.1.
DR AlphaFoldDB; A0A0Q6XES4; -.
DR STRING; 1736433.ASC87_02205; -.
DR OrthoDB; 9762009at2; -.
DR Proteomes; UP000051465; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000051465};
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 284..311
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 394..413
FT /note="Disordered"
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 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 413 AA; 46754 MW; 72CEBB1EA21E70A3 CRC64;
MNARWTTGNR FELLENGEAF FPAVFDAIRH AKHEVVLETF IVFEDKVGWE LHAALVEAGR
RGVSVDVLVD GFGSSELTPA FIGPLAGAGV RLRAFDPKPR FLGMRTNVFR RMHRKIVVVD
QAVAFVGGLN YSADHLADFG PQAKQDYAVK VEGPIVAEIH TFARAAIANA DPRRHWFRRE
HDPQRQTGSE AAALFVTRDN QDHRTDIERH YRVAIRAARK EVTIANAYFF PGYRLLKEMR
RAARRGVRVR LILQGEPDMP IVKTAAAMLY DHLQRAGVQI YEYCARPLHG KVALTDDEWS
TVGSSNLDPL SLSLNLEANL FIRDRAFNRH LRERLEALIE NGCQQISADR LPARNVFHLV
RSFFVFHFLR RYPAWAGWLP AHVPKVVTPQ VDDHPGAASL EGMTRVTETP EAR
//
