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Database: UniProt
Entry: Q1LDQ3_CUPMC
LinkDB: Q1LDQ3_CUPMC
Original site: Q1LDQ3_CUPMC 
ID   Q1LDQ3_CUPMC            Unreviewed;       210 AA.
AC   Q1LDQ3;
DT   30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   30-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   RecName: Full=CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase {ECO:0000256|ARBA:ARBA00014944};
DE            EC=2.7.8.5 {ECO:0000256|ARBA:ARBA00013170};
GN   OrderedLocusNames=Rmet_4861 {ECO:0000313|EMBL:ABF11723.1};
OS   Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS   CH34) (Ralstonia metallidurans).
OG   Plasmid megaplasmid CH34 {ECO:0000313|Proteomes:UP000002429}.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=266264 {ECO:0000313|EMBL:ABF11723.1, ECO:0000313|Proteomes:UP000002429};
RN   [1] {ECO:0000313|Proteomes:UP000002429}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34
RC   {ECO:0000313|Proteomes:UP000002429};
RC   PLASMID=Plasmid megaplasmid CH34 {ECO:0000313|Proteomes:UP000002429};
RX   PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA   Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA   Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA   Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT   "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT   master survivalist in harsh and anthropogenic environments.";
RL   PLoS ONE 5:E10433-E10433(2010).
CC   -!- FUNCTION: This protein catalyzes the committed step to the synthesis of
CC       the acidic phospholipids. {ECO:0000256|ARBA:ARBA00003973}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-
CC         diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + CMP +
CC         H(+); Xref=Rhea:RHEA:12593, ChEBI:CHEBI:15378, ChEBI:CHEBI:57597,
CC         ChEBI:CHEBI:58332, ChEBI:CHEBI:60110, ChEBI:CHEBI:60377; EC=2.7.8.5;
CC         Evidence={ECO:0000256|ARBA:ARBA00001566};
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylglycerol biosynthesis;
CC       phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
CC       {ECO:0000256|ARBA:ARBA00005042}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC       family. {ECO:0000256|ARBA:ARBA00010441, ECO:0000256|RuleBase:RU003750}.
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DR   EMBL; CP000353; ABF11723.1; -; Genomic_DNA.
DR   RefSeq; WP_011519284.1; NC_007974.2.
DR   AlphaFoldDB; Q1LDQ3; -.
DR   DNASU; 4041723; -.
DR   KEGG; rme:Rmet_4861; -.
DR   eggNOG; COG1183; Bacteria.
DR   HOGENOM; CLU_049944_5_2_4; -.
DR   Proteomes; UP000002429; Plasmid megaplasmid CH34.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008444; F:CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity; IEA:RHEA.
DR   GO; GO:0003882; F:CDP-diacylglycerol-serine O-phosphatidyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.120.1760; -; 1.
DR   InterPro; IPR000462; CDP-OH_P_trans.
DR   InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR   InterPro; IPR048254; CDP_ALCOHOL_P_TRANSF_CS.
DR   PANTHER; PTHR14269; CDP-DIACYLGLYCEROL--GLYCEROL-3-PHOSPHATE 3-PHOSPHATIDYLTRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR14269:SF61; CDP-DIACYLGLYCEROL--SERINE O-PHOSPHATIDYLTRANSFERASE; 1.
DR   Pfam; PF01066; CDP-OH_P_transf; 1.
DR   PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1.
PE   3: Inferred from homology;
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW   Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW   Plasmid {ECO:0000313|EMBL:ABF11723.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002429};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003750};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        49..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   210 AA;  22498 MW;  FF241E562F26817C CRC64;
     MSTPQPRPRH FSMLRDLQLA DFFTLANAAC GMGSVFFAMF FVAEPSLRTF YIAAALAPAA
     FIFDVLDGRI ARWRHAHSAL GRELDSLSDI ISFGVGPATL AFAAGMRGGW DLAALIYFVC
     CGVSRLARFN VTAESMAEGT GKVKYFEGTP IPTSVVLTGV LAWCASQGRI GDALVGGAWE
     IGPGTLHPMA LLFVLSGSLM ISKTLRIPKF
//
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