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Database: UniProt
Entry: Q7NYG8_CHRVO
LinkDB: Q7NYG8_CHRVO
Original site: Q7NYG8_CHRVO 
ID   Q7NYG8_CHRVO            Unreviewed;       193 AA.
AC   Q7NYG8;
DT   15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2003, sequence version 1.
DT   27-MAR-2024, entry version 118.
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:AAQ58981.1};
GN   OrderedLocusNames=CV_1306 {ECO:0000313|EMBL:AAQ58981.1};
OS   Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC
OS   12614 / NCIMB 9131 / NCTC 9757).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Chromobacteriaceae; Chromobacterium.
OX   NCBI_TaxID=243365 {ECO:0000313|EMBL:AAQ58981.1, ECO:0000313|Proteomes:UP000001424};
RN   [1] {ECO:0000313|EMBL:AAQ58981.1, ECO:0000313|Proteomes:UP000001424}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 /
RC   NCTC 9757 {ECO:0000313|Proteomes:UP000001424};
RX   PubMed=14500782; DOI=10.1073/pnas.1832124100;
RA   Vasconcelos A.T.R., de Almeida D.F., Almeida F.C., de Almeida L.G.P.,
RA   de Almeida R., Goncalves J.A.A., Andrade E.M., Antonio R.V., Araripe J.,
RA   de Araujo M.F.F., Filho S.A., Azevedo V., Batista A.J., Bataus L.A.M.,
RA   Batista J.S., Belo A., vander Berg C., Blamey J., Bogo M., Bonato S.,
RA   Bordignon J., Brito C.A., Brocchi M., Burity H.A., Camargo A.A.,
RA   Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B.,
RA   Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Pasa T.B.C., Duran N.,
RA   Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S.,
RA   Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A.,
RA   Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B.,
RA   Grattapaglia D., Grisard E.C., Guimaraes C.T., Hanna E.S., Hungria M.,
RA   Jardim S.N., Laurino J., Leoi L.C.T., Fassarella L., Lima A.,
RA   Loureiro M.F., Lyra M.C.P., Macedo M., Madeira H.M.F., Manfio G.P.,
RA   Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B.,
RA   Meissner R.D.V., Menck C.F.M., Moreira M.A.M., Nascimento F.F.,
RA   Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A.,
RA   Pedrosa F.O., Pena S.J.D., Perreira J.O., Perreira M., Pinto L.S.R.C.,
RA   Pinto L.S., Porto J.I.R., Potrich D.P., Neto C.E.R., Reis A.M.M.,
RA   Rigo L.U., Rondinelli E., dos Santos E.B.P., Santos F.R., Schneider M.P.C.,
RA   Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R.,
RA   Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M.,
RA   Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R.,
RA   Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.;
RT   "The complete genome sequence of Chromobacterium violaceum reveals
RT   remarkable and exploitable bacterial adaptability.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003).
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; AE016825; AAQ58981.1; -; Genomic_DNA.
DR   RefSeq; WP_011134860.1; NC_005085.1.
DR   AlphaFoldDB; Q7NYG8; -.
DR   STRING; 243365.CV_1306; -.
DR   GeneID; 66366967; -.
DR   KEGG; cvi:CV_1306; -.
DR   eggNOG; COG0558; Bacteria.
DR   HOGENOM; CLU_051314_2_1_4; -.
DR   OrthoDB; 9796672at2; -.
DR   Proteomes; UP000001424; Chromosome.
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:SF62; CDP-DIACYLGLYCEROL--GLYCEROL-3-PHOSPHATE 3-PHOSPHATIDYLTRANSFERASE 1, CHLOROPLASTIC; 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:UP000001424};
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        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        38..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        78..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        124..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        158..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   193 AA;  20835 MW;  E743A28FE31F3163 CRC64;
     MPFNLPILLT WLRVALIPIC VAVFFLPDSI LLLHSRNAVG AGIFALAAAT DWLDGYLARK
     LGQTSAFGAF LDPVADKLIV AAALILLVQL GRTEGWMAMI IIGREITISA LREWMAGMGS
     RSSVAVAYIG KLKTAAQMLA ITLLLYDGAL VPGLDARGLG NFSMYVAVIL TLWSMIYYLQ
     MAAKEFAGKK IDV
//
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