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Database: UniProt
Entry: A0A0M7B8W8_9RHOB
LinkDB: A0A0M7B8W8_9RHOB
Original site: A0A0M7B8W8_9RHOB 
ID   A0A0M7B8W8_9RHOB        Unreviewed;       222 AA.
AC   A0A0M7B8W8;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
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   Name=pgsA {ECO:0000313|EMBL:CUH35189.1};
GN   ORFNames=JSE7799_01098 {ECO:0000313|EMBL:CUH35189.1};
OS   Jannaschia seosinensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Jannaschia.
OX   NCBI_TaxID=313367 {ECO:0000313|EMBL:CUH35189.1, ECO:0000313|Proteomes:UP000049455};
RN   [1] {ECO:0000313|EMBL:CUH35189.1, ECO:0000313|Proteomes:UP000049455}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7799 {ECO:0000313|EMBL:CUH35189.1,
RC   ECO:0000313|Proteomes:UP000049455};
RA   Jackson K.R., Lunt B.L., Fisher J.N.B., Gardner A.V., Bailey M.E.,
RA   Deus L.M., Earl A.S., Gibby P.D., Hartmann K.A., Liu J.E., Manci A.M.,
RA   Nielsen D.A., Solomon M.B., Breakwell D.P., Burnett S.H., Grose J.H.;
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylglycerol biosynthesis;
CC       phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
CC       {ECO:0000256|ARBA:ARBA00005042}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {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; CYPR01000060; CUH35189.1; -; Genomic_DNA.
DR   RefSeq; WP_055662736.1; NZ_CYPR01000060.1.
DR   AlphaFoldDB; A0A0M7B8W8; -.
DR   STRING; 313367.JSE7799_01098; -.
DR   OrthoDB; 9796672at2; -.
DR   Proteomes; UP000049455; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008444; F:CDP-diacylglycerol-glycerol-3-phosphate 3-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   InterPro; IPR004570; Phosphatidylglycerol_P_synth.
DR   NCBIfam; TIGR00560; pgsA; 1.
DR   PANTHER; PTHR14269:SF60; CARDIOLIPIN SYNTHASE (CMP-FORMING); 1.
DR   PANTHER; PTHR14269; CDP-DIACYLGLYCEROL--GLYCEROL-3-PHOSPHATE 3-PHOSPHATIDYLTRANSFERASE-RELATED; 1.
DR   Pfam; PF01066; CDP-OH_P_transf; 1.
DR   PIRSF; PIRSF000847; Phos_ph_gly_syn; 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   Reference proteome {ECO:0000313|Proteomes:UP000049455};
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        7..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        34..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        74..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        188..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   222 AA;  24688 MW;  6F7931911EF12B36 CRC64;
     MTWTIPNLLT VLRLLAAPGV AIMFLFFARP WADWFALILF ITAAVTDWFD GYLAREWQQE
     TRFGAMLDPI ADKAMVVIAL LVITGFSGMN PWILLPATVI LFREVFVSGL REFLGNTASL
     LKVTNLAKWK TTAQMVSIAV LFATGVFEHA FAERVQGMDP ATIDAIMTGA MPDEIGIVRL
     EQGEQVTFAI GVLLLWIAAA LTAWTGWDYF SKAMPHLRDR TS
//
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