PCS_PSEAE
ID PCS_PSEAE Reviewed; 238 AA.
AC Q9HXE9;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Phosphatidylcholine synthase {ECO:0000303|PubMed:12169604, ECO:0000303|PubMed:14663079, ECO:0000312|EMBL:AAG07244.1};
DE Short=PC synthase {ECO:0000250|UniProtKB:Q9KJY8};
DE Short=PCS {ECO:0000303|PubMed:12169604, ECO:0000303|PubMed:14663079};
DE EC=2.7.8.24 {ECO:0000269|PubMed:12169604, ECO:0000269|PubMed:14663079};
DE AltName: Full=CDP-diglyceride-choline O-phosphatidyltransferase {ECO:0000303|PubMed:12169604};
GN Name=pcs {ECO:0000312|EMBL:AAG07244.1}; OrderedLocusNames=PA3857;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1] {ECO:0000312|EMBL:AAG07244.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2] {ECO:0000305}
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1 {ECO:0000269|PubMed:12169604};
RX PubMed=12169604; DOI=10.1128/jb.184.17.4792-4799.2002;
RA Wilderman P.J., Vasil A.I., Martin W.E., Murphy R.C., Vasil M.L.;
RT "Pseudomonas aeruginosa synthesizes phosphatidylcholine by use of the
RT phosphatidylcholine synthase pathway.";
RL J. Bacteriol. 184:4792-4799(2002).
RN [3] {ECO:0000305}
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1 {ECO:0000269|PubMed:14663079};
RX PubMed=14663079; DOI=10.1099/mic.0.26522-0;
RA Martinez-Morales F., Schobert M., Lopez-Lara I.M., Geiger O.;
RT "Pathways for phosphatidylcholine biosynthesis in bacteria.";
RL Microbiology 149:3461-3471(2003).
CC -!- FUNCTION: Condenses choline with CDP-diglyceride to produce
CC phosphatidylcholine and CMP. {ECO:0000269|PubMed:12169604,
CC ECO:0000269|PubMed:14663079}.
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:0000269|PubMed:12169604, ECO:0000269|PubMed:14663079};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9KJY8};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:Q9KJY8}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9KJY8}.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000255}.
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DR EMBL; AE004091; AAG07244.1; -; Genomic_DNA.
DR PIR; D83165; D83165.
DR RefSeq; NP_252546.1; NC_002516.2.
DR RefSeq; WP_003105024.1; NZ_QZGE01000001.1.
DR AlphaFoldDB; Q9HXE9; -.
DR SMR; Q9HXE9; -.
DR STRING; 287.DR97_4009; -.
DR PaxDb; Q9HXE9; -.
DR DNASU; 879785; -.
DR EnsemblBacteria; AAG07244; AAG07244; PA3857.
DR GeneID; 879785; -.
DR KEGG; pae:PA3857; -.
DR PATRIC; fig|208964.12.peg.4038; -.
DR PseudoCAP; PA3857; -.
DR HOGENOM; CLU_086279_0_0_6; -.
DR InParanoid; Q9HXE9; -.
DR OMA; FLHPFRV; -.
DR PhylomeDB; Q9HXE9; -.
DR BioCyc; PAER208964:G1FZ6-3928-MON; -.
DR BRENDA; 2.7.8.24; 5087.
DR Proteomes; UP000002438; Chromosome.
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:0050520; F:phosphatidylcholine synthase activity; IDA:UniProtKB.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Lipid biosynthesis; Lipid metabolism;
KW Manganese; Membrane; Phospholipid biosynthesis; Phospholipid metabolism;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..238
FT /note="Phosphatidylcholine synthase"
FT /id="PRO_0000425222"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9KJY8, ECO:0000255"
FT TRANSMEM 17..37
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..41
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..75
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..104
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..132
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 154..155
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..183
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 205..209
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9KJY8, ECO:0000255"
SQ SEQUENCE 238 AA; 26649 MW; C5DDCAD47FE5BB7B CRC64;
MPVNLSMTPI NKAKAWGVHA VTASGVILAL LALLALVDNK PQACLLWLGL ALLVDGLDGT
LARKYEVKEM LPHFDGSVLD LVIDYLTYVF IPAIFIYRYI PLPEHFELLA VGVILVSSLF
CFCNVNMKST DNYFVGFPAA WNVVAVYFYV LDLHPWVNLA TVLVLAALTL TRMKFLHPFR
VRQFMPLNIA VTFVWLISSG LLIVQQPADL PILLGLWFAA SAYFVGICLW RSAREWFG
