PCS_LEGBO
ID PCS_LEGBO Reviewed; 217 AA.
AC D5KX81;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 25-MAY-2022, entry version 22.
DE RecName: Full=Phosphatidylcholine synthase {ECO:0000303|PubMed:20338739, ECO:0000312|EMBL:ADE20140.1};
DE Short=PC synthase {ECO:0000250|UniProtKB:Q9KJY8};
DE Short=PCS {ECO:0000303|PubMed:20338739};
DE EC=2.7.8.24 {ECO:0000269|PubMed:20338739};
DE AltName: Full=CDP-diglyceride-choline O-phosphatidyltransferase {ECO:0000250|UniProtKB:Q9KJY8};
DE Flags: Fragment;
GN Name=pcsA {ECO:0000312|EMBL:ADE20140.1};
OS Legionella bozemanae (Fluoribacter bozemanae).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=447;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ADE20140.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 33217 / DSM 16523 / CCUG 11880 / NCTC 11368 / WIGA
RC {ECO:0000312|EMBL:ADE20140.1};
RX PubMed=20338739; DOI=10.1016/j.micres.2010.02.004;
RA Palusinska-Szysz M., Janczarek M., Kalitynski R., Dawidowicz A.L.,
RA Russa R.;
RT "Legionella bozemanae synthesizes phosphatidylcholine from exogenous
RT choline.";
RL Microbiol. Res. 166:87-98(2011).
CC -!- FUNCTION: Condenses choline with CDP-diglyceride to produce
CC phosphatidylcholine and CMP. {ECO:0000269|PubMed:20338739}.
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:20338739};
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; GU647106; ADE20140.1; -; Genomic_DNA.
DR AlphaFoldDB; D5KX81; -.
DR STRING; 447.Lboz_0037; -.
DR BRENDA; 2.7.8.24; 13323.
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; IEA:UniProtKB-EC.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
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 Transferase; Transmembrane; Transmembrane helix.
FT CHAIN <1..>217
FT /note="Phosphatidylcholine synthase"
FT /id="PRO_0000425220"
FT TRANSMEM <1..8
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 9..16
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q5ZV56, ECO:0000305"
FT TRANSMEM 17..37
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:Q5ZV56, ECO:0000305"
FT TOPO_DOM 38..50
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q5ZV56, ECO:0000305"
FT TRANSMEM 51..71
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:Q5ZV56, ECO:0000305"
FT TOPO_DOM 72..77
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q5ZV56, ECO:0000305"
FT TRANSMEM 78..98
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:Q5ZV56, ECO:0000305"
FT TOPO_DOM 99..107
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q5ZV56, ECO:0000305"
FT TRANSMEM 108..128
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:Q5ZV56, ECO:0000305"
FT TOPO_DOM 129
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q5ZV56, ECO:0000305"
FT TRANSMEM 130..149
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:Q5ZV56, ECO:0000305"
FT TOPO_DOM 150..164
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q5ZV56, ECO:0000305"
FT TRANSMEM 165..185
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:Q5ZV56, ECO:0000305"
FT TOPO_DOM 186..191
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q5ZV56, ECO:0000305"
FT TRANSMEM 192..212
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250|UniProtKB:Q5ZV56, ECO:0000305"
FT TOPO_DOM 213..>217
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q5ZV56,
FT ECO:0000250|UniProtKB:Q9KJY8, ECO:0000305"
FT NON_TER 1
FT /evidence="ECO:0000312|EMBL:ADE20140.1"
FT NON_TER 217
FT /evidence="ECO:0000312|EMBL:ADE20140.1"
SQ SEQUENCE 217 AA; 24771 MW; 0A04F0ADCA41990C CRC64;
ACIGVFSLVK IYQHEYIFAL WLMFITVVID AVDGTLARLV NIKKILPKID GALLDNIVDY
LNYVITPCFF LLVKPGMLPP EYSVFLIAAV SITSAYQFCQ CDAKTPDHFF KGFPCYWNIT
ILYMFIFNTS AATNAIILII LSILIFVPVK YVYPSRLDYL TESRILKILM HICSIIYAVS
SICILISYPN TNIICLSLSV AYVGMYLFLS FYRTYYP
