PCS_BORBU
ID PCS_BORBU Reviewed; 234 AA.
AC O51265;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Phosphatidylcholine synthase {ECO:0000303|PubMed:14663079, ECO:0000303|PubMed:14766917};
DE Short=PC synthase {ECO:0000250|UniProtKB:Q9KJY8};
DE Short=PCS {ECO:0000303|PubMed:14663079, ECO:0000303|PubMed:14766917};
DE EC=2.7.8.24 {ECO:0000269|PubMed:14663079, ECO:0000269|PubMed:14766917};
DE AltName: Full=CDP-diglyceride-choline O-phosphatidyltransferase {ECO:0000250|UniProtKB:Q9KJY8, ECO:0000312|EMBL:AAB91497.1};
GN Name=pcs {ECO:0000303|PubMed:14766917}; OrderedLocusNames=BB_0249;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=224326;
RN [1] {ECO:0000312|EMBL:AAB91497.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(1997).
RN [2] {ECO:0000305}
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31
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=ATCC 35210 / DSM 4680 / CIP 102532 / B31
RC {ECO:0000269|PubMed:14766917};
RX PubMed=14766917; DOI=10.1099/mic.0.26752-0;
RA Wang X.G., Scagliotti J.P., Hu L.T.;
RT "Phospholipid synthesis in Borrelia burgdorferi: BB0249 and BB0721 encode
RT functional phosphatidylcholine synthase and phosphatidylglycerolphosphate
RT synthase proteins.";
RL Microbiology 150:391-397(2004).
CC -!- FUNCTION: Condenses choline with CDP-diglyceride to produce
CC phosphatidylcholine and CMP. {ECO:0000269|PubMed:14663079,
CC ECO:0000269|PubMed:14766917}.
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:14766917};
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; AE000783; AAB91497.1; -; Genomic_DNA.
DR PIR; A70131; A70131.
DR RefSeq; NP_212383.1; NC_001318.1.
DR RefSeq; WP_002556848.1; NC_001318.1.
DR AlphaFoldDB; O51265; -.
DR STRING; 224326.BB_0249; -.
DR PRIDE; O51265; -.
DR EnsemblBacteria; AAB91497; AAB91497; BB_0249.
DR GeneID; 56567679; -.
DR KEGG; bbu:BB_0249; -.
DR PATRIC; fig|224326.49.peg.648; -.
DR HOGENOM; CLU_086279_0_0_12; -.
DR OMA; FLHPFRV; -.
DR BRENDA; 2.7.8.24; 902.
DR Proteomes; UP000001807; 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..234
FT /note="Phosphatidylcholine synthase"
FT /id="PRO_0000425217"
FT TOPO_DOM 1..3
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9KJY8, ECO:0000255"
FT TRANSMEM 4..24
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..26
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 27..47
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 48..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..98
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..116
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..126
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 148..149
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..180
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 202..207
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..234
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9KJY8, ECO:0000255"
SQ SEQUENCE 234 AA; 26678 MW; 968A205282E3623D CRC64;
MKNINLILAW LVHIFTASGL IVGLYSIISI VNGNYSLLLK LTVIGLIIDG IDGTMARKLK
VKELIPEIDG TLLDNITDYI NYTFIPVIFF YLGEFIEEKY KVAICIGILL SSAYQFSRTD
AKTNDNYFRG FPSLWNLFVI LNIIFKMEQI TNLITMSICI ITSFIPIKFI YPSKTKELRK
ITIPITIISC LIFVVSIFSE LSTTALKMAK TVLILYFAYL TLASIYLTYK TRNR
