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Database: UniProt
Entry: S9QLD1_9RHOB
LinkDB: S9QLD1_9RHOB
Original site: S9QLD1_9RHOB 
ID   S9QLD1_9RHOB            Unreviewed;       237 AA.
AC   S9QLD1;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=Phosphatidylcholine synthase {ECO:0000256|ARBA:ARBA00015623, ECO:0000256|PIRNR:PIRNR000851};
DE            Short=PC synthase {ECO:0000256|PIRNR:PIRNR000851};
DE            Short=PCS {ECO:0000256|PIRNR:PIRNR000851};
DE            EC=2.7.8.24 {ECO:0000256|ARBA:ARBA00013195, ECO:0000256|PIRNR:PIRNR000851};
DE   AltName: Full=CDP-diglyceride-choline O-phosphatidyltransferase {ECO:0000256|ARBA:ARBA00033321, ECO:0000256|PIRNR:PIRNR000851};
GN   ORFNames=Salmuc_03053 {ECO:0000313|EMBL:EPX82266.1};
OS   Salipiger mucosus DSM 16094.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Salipiger.
OX   NCBI_TaxID=1123237 {ECO:0000313|EMBL:EPX82266.1, ECO:0000313|Proteomes:UP000015347};
RN   [1] {ECO:0000313|Proteomes:UP000015347}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16094 {ECO:0000313|Proteomes:UP000015347};
RX   PubMed=25197501; DOI=10.4056/sigs.4909790;
RA   Riedel T., Spring S., Fiebig A., Petersen J., Kyrpides N.C., Goker M.,
RA   Klenk H.P.;
RT   "Genome sequence of the exopolysaccharide-producing Salipiger mucosus type
RT   strain (DSM 16094(T)), a moderately halophilic member of the Roseobacter
RT   clade.";
RL   Stand. Genomic Sci. 9:1331-1343(2014).
CC   -!- FUNCTION: Condenses choline with CDP-diglyceride to produce
CC       phosphatidylcholine and CMP. {ECO:0000256|ARBA:ARBA00037468,
CC       ECO:0000256|PIRNR:PIRNR000851}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a CDP-1,2-diacyl-sn-glycerol + choline = a 1,2-diacyl-sn-
CC         glycero-3-phosphocholine + CMP + H(+); Xref=Rhea:RHEA:14597,
CC         ChEBI:CHEBI:15354, ChEBI:CHEBI:15378, ChEBI:CHEBI:57643,
CC         ChEBI:CHEBI:58332, ChEBI:CHEBI:60377; EC=2.7.8.24;
CC         Evidence={ECO:0000256|ARBA:ARBA00000958,
CC         ECO:0000256|PIRNR:PIRNR000851};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936,
CC         ECO:0000256|PIRNR:PIRNR000851};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004429, ECO:0000256|PIRNR:PIRNR000851}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004429,
CC       ECO:0000256|PIRNR:PIRNR000851}. 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|PIRNR:PIRNR000851}.
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:EPX82266.1}.
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DR   EMBL; APVH01000024; EPX82266.1; -; Genomic_DNA.
DR   AlphaFoldDB; S9QLD1; -.
DR   STRING; 1123237.Salmuc_03053; -.
DR   eggNOG; COG1183; Bacteria.
DR   HOGENOM; CLU_086279_0_0_5; -.
DR   Proteomes; UP000015347; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0050520; F:phosphatidylcholine synthase 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; IPR026027; PcS.
DR   Pfam; PF01066; CDP-OH_P_transf; 1.
DR   PIRSF; PIRSF000851; PcS; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane {ECO:0000256|ARBA:ARBA00022519,
KW   ECO:0000256|PIRNR:PIRNR000851};
KW   Cell membrane {ECO:0000256|PIRNR:PIRNR000851};
KW   Lipid biosynthesis {ECO:0000256|PIRNR:PIRNR000851};
KW   Lipid metabolism {ECO:0000256|PIRNR:PIRNR000851};
KW   Manganese {ECO:0000256|PIRNR:PIRNR000851};
KW   Membrane {ECO:0000256|PIRNR:PIRNR000851, ECO:0000256|SAM:Phobius};
KW   Phospholipid biosynthesis {ECO:0000256|PIRNR:PIRNR000851};
KW   Phospholipid metabolism {ECO:0000256|PIRNR:PIRNR000851};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015347};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000851, ECO:0000313|EMBL:EPX82266.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        39..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        75..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        103..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        185..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        209..228
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   237 AA;  26461 MW;  D3BEEBE80614A3CA CRC64;
     MGHDIGMTLG TRALLVHLLT ATGAVFAMLA LLAAAQEQWS IMFLWLVVAF AVDGFDGPLA
     RKYDVKTNAP RFDGVLLDLI IDYLTYVFIP AFALFQSDLL PGWTGWIAII VITFASALYF
     ADSRMKTDDN SFHGFPGCWN MLVIVLFAIK PAFWLILLLV AVLAVAMFLP LKFIHPVRTA
     RWRALSLPLA LAWTFFAGWA AWVDFHPESW AHWGLVTTSV YLVFAGIAQQ VIPQRRG
//
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