ID I8I5C8_9GAMM Unreviewed; 425 AA.
AC I8I5C8;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=WQQ_17330 {ECO:0000313|EMBL:EIT71596.1};
OS Hydrocarboniphaga effusa AP103.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Nevskiales; Nevskiaceae;
OC Hydrocarboniphaga.
OX NCBI_TaxID=1172194 {ECO:0000313|EMBL:EIT71596.1, ECO:0000313|Proteomes:UP000003704};
RN [1] {ECO:0000313|EMBL:EIT71596.1, ECO:0000313|Proteomes:UP000003704}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP103 {ECO:0000313|EMBL:EIT71596.1,
RC ECO:0000313|Proteomes:UP000003704};
RX PubMed=22933753; DOI=10.1128/JB.01017-12;
RA Chang H.K., Zylstra G.J., Chae J.C.;
RT "Genome Sequence of n-Alkane-Degrading Hydrocarboniphaga effusa Strain
RT AP103T (ATCC BAA-332T).";
RL J. Bacteriol. 194:5120-5120(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:EIT71596.1}.
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DR EMBL; AKGD01000001; EIT71596.1; -; Genomic_DNA.
DR RefSeq; WP_007184682.1; NZ_AKGD01000001.1.
DR AlphaFoldDB; I8I5C8; -.
DR STRING; 1172194.WQQ_17330; -.
DR PATRIC; fig|1172194.4.peg.1674; -.
DR OrthoDB; 9762009at2; -.
DR Proteomes; UP000003704; 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; 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:UP000003704};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01917}.
FT DOMAIN 112..139
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 296..323
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 395..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 117
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 119
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 124
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 301
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 303
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
FT ACT_SITE 308
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01917"
SQ SEQUENCE 425 AA; 49103 MW; B65A14B17FE6E798 CRC64;
MKDDRRHPWR AGNRVQLLEN GEAYYPRVLE IVNAAEKEIF VETFILFDDP VGKPFQQALI
AAARRGCRVE LTVDGYGSAN LTPEFIGEMT SVGIQFHVYR PQPKVMGMRT NLFRRLHRKL
IVVDGRIAFC GGINIAFDHV ADFGPTSKQD YAVEVEGPIV RDIHRFVELS VAKSEAKQNR
LKRWWQRRKQ AIPEPEHASV GSVNAMFVIR DNERHHDDIE RQYRLAIKSA RSRIVIANAY
FFPGWRLLRN LRDAARRGVD VTLILQGKPD MWYVKWVAEN LYHYLMKAGV RIYEYCERPL
HAKVAVIDDH WATVGSSNLD PLSLYLNLES NLVFRDAAFN AHLASRLRHL MQQCCREVQW
DSIPHRDIRR QLFVFITYHL GRRFPAWAGW RPAHAQKQGI AAPDSRPPDD QREAPGSLQA
QSAKH
//