PGSA_CERS4
ID PGSA_CERS4 Reviewed; 221 AA.
AC Q3IYX7; Q53090;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase;
DE EC=2.7.8.5;
DE AltName: Full=Phosphatidylglycerophosphate synthase;
DE Short=PGP synthase;
GN Name=pgsA; OrderedLocusNames=RHOS4_26890; ORFNames=RSP_1073;
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=272943;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8576035; DOI=10.1128/jb.178.4.1030-1038.1996;
RA Dryden S.C., Dowhan W.;
RT "Isolation and expression of the Rhodobacter sphaeroides gene (pgsA)
RT encoding phosphatidylglycerophosphate synthase.";
RL J. Bacteriol. 178:1030-1038(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: This protein catalyzes the committed step to the synthesis of
CC the acidic phospholipids. {ECO:0000269|PubMed:8576035}.
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 -!- PATHWAY: Phospholipid metabolism; phosphatidylglycerol biosynthesis;
CC phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8576035};
CC Multi-pass membrane protein {ECO:0000269|PubMed:8576035}.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC44003.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U29587; AAC44003.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP000143; ABA80257.1; -; Genomic_DNA.
DR RefSeq; WP_002721439.1; NZ_CP030271.1.
DR RefSeq; YP_354158.1; NC_007493.2.
DR AlphaFoldDB; Q3IYX7; -.
DR SMR; Q3IYX7; -.
DR STRING; 272943.RSP_1073; -.
DR EnsemblBacteria; ABA80257; ABA80257; RSP_1073.
DR GeneID; 57471407; -.
DR GeneID; 67447847; -.
DR KEGG; rsp:RSP_1073; -.
DR PATRIC; fig|272943.9.peg.3047; -.
DR eggNOG; COG0558; Bacteria.
DR OMA; WSMVYYL; -.
DR PhylomeDB; Q3IYX7; -.
DR UniPathway; UPA00084; UER00503.
DR Proteomes; UP000002703; Chromosome 1.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008444; F:CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006655; P:phosphatidylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.20.120.1760; -; 1.
DR InterPro; IPR000462; CDP-OH_P_trans.
DR InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR InterPro; IPR004570; Phosphatidylglycerol_P_synth.
DR Pfam; PF01066; CDP-OH_P_transf; 1.
DR PIRSF; PIRSF000847; Phos_ph_gly_syn; 1.
DR TIGRFAMs; TIGR00560; pgsA; 1.
DR PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1.
PE 3: Inferred from homology;
KW Cell membrane; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..221
FT /note="CDP-diacylglycerol--glycerol-3-phosphate 3-
FT phosphatidyltransferase"
FT /id="PRO_0000239137"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 221 AA; 24683 MW; CD9E26A04270B411 CRC64;
MNWSIPNILT VLRLLAAPGV AVMFLYFHRP WADWFALTLF ILAAVTDFFD GYLARLWKQE
SKFGAMLDPI ADKAMVVIAL VIITGYSGMN PWLILPVTLI LFREVFVSGL REFLGAKASL
LKVTKLAKWK TTAQMVAIAI LFLGTGLEHL EGIARQGMTW EQYARAVSAG EADPIRSCGM
HGCSSYATWL GLALIWIAAA LTFITGWDYF RKALPYLKDE K
