PCS_LEGPH
ID PCS_LEGPH Reviewed; 255 AA.
AC Q5ZV56;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Phosphatidylcholine synthase {ECO:0000303|PubMed:14663079};
DE Short=PC synthase {ECO:0000250|UniProtKB:Q9KJY8};
DE Short=PCS {ECO:0000303|PubMed:14663079};
DE EC=2.7.8.24 {ECO:0000269|PubMed:14663079, ECO:0000269|PubMed:17979985, ECO:0000312|EMBL:AAU27666.1};
DE AltName: Full=CDP-diglyceride-choline O-phosphatidyltransferase {ECO:0000250|UniProtKB:Q9KJY8, ECO:0000312|EMBL:AAU27666.1};
GN Name=pcsA {ECO:0000303|PubMed:17979985}; OrderedLocusNames=lpg1584;
OS Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS 33152 / DSM 7513).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=272624;
RN [1] {ECO:0000312|EMBL:AAU27666.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX PubMed=15448271; DOI=10.1126/science.1099776;
RA Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA Russo J.J.;
RT "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL Science 305:1966-1968(2004).
RN [2] {ECO:0000305}
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513
RC {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).
RN [3] {ECO:0000305}
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513
RC {ECO:0000269|PubMed:17979985};
RX PubMed=17979985; DOI=10.1111/j.1462-5822.2007.01066.x;
RA Conover G.M., Martinez-Morales F., Heidtman M.I., Luo Z.Q., Tang M.,
RA Chen C., Geiger O., Isberg R.R.;
RT "Phosphatidylcholine synthesis is required for optimal function of
RT Legionella pneumophila virulence determinants.";
RL Cell. Microbiol. 10:514-528(2008).
CC -!- FUNCTION: Condenses choline with CDP-diglyceride to produce
CC phosphatidylcholine and CMP. Affects virulence of this bacterium when
CC there is a complete loss of phosphatidylcholine formation due to
CC absence of both the synthase (pcs) and the methylation (pmtA) pathways.
CC Reduced virulence results from lowered yields of bacteria within host
CC macrophages and because of loss of high multiplicity cytotoxicity.
CC {ECO:0000269|PubMed:14663079, ECO:0000269|PubMed:17979985}.
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:14663079, ECO:0000269|PubMed:17979985};
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; AE017354; AAU27666.1; -; Genomic_DNA.
DR RefSeq; WP_010947313.1; NC_002942.5.
DR RefSeq; YP_095613.1; NC_002942.5.
DR AlphaFoldDB; Q5ZV56; -.
DR SMR; Q5ZV56; -.
DR STRING; 272624.lpg1584; -.
DR PaxDb; Q5ZV56; -.
DR DNASU; 3077993; -.
DR EnsemblBacteria; AAU27666; AAU27666; lpg1584.
DR GeneID; 66490716; -.
DR KEGG; lpn:lpg1584; -.
DR PATRIC; fig|272624.6.peg.1660; -.
DR eggNOG; COG1183; Bacteria.
DR HOGENOM; CLU_086279_0_0_6; -.
DR OMA; FLHPFRV; -.
DR Proteomes; UP000000609; 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; IPR043130; CDP-OH_PTrfase_TM_dom.
DR InterPro; IPR026027; PcS.
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..255
FT /note="Phosphatidylcholine synthase"
FT /id="PRO_0000425221"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9KJY8, ECO:0000255"
FT TRANSMEM 14..34
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..42
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..63
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..76
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255, ECO:0000305"
FT TOPO_DOM 98..103
FT /note="Periplasmic"
FT /evidence="ECO:0000255, ECO:0000305"
FT TRANSMEM 104..124
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255, ECO:0000305"
FT TOPO_DOM 125..133
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255, ECO:0000305"
FT TRANSMEM 134..154
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 155
FT /note="Periplasmic"
FT /evidence="ECO:0000255, ECO:0000305"
FT TRANSMEM 156..175
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255, ECO:0000305"
FT TOPO_DOM 176..190
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..217
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..255
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9KJY8, ECO:0000255"
SQ SEQUENCE 255 AA; 29268 MW; 32CC0A13E272E19B CRC64;
MNPIKPPFTL NQYFAAWFVH VFTASAACIG VFSLYKIYQH DYVFALWLMA ITVFIDAVDG
SLARLVHVKS VLPKIDGALL DNIVDYLNYV ITPCFFLLVK PGMLPADYVV PITAAITITS
AYQFCQDDAK TPDHFFKGFP CYWNITVFYM YIFNTSMIVN TVLLSLFCVL IFIPVKYVYP
SRLDYLTESR VLKILMHCCS ALYGISSFCL LVNYPETNKL WVSLSLGYVG MYLFLSFYRT
YYPMFKAKIT ANNKD
