PCS_RHILO
ID PCS_RHILO Reviewed; 268 AA.
AC Q98MN3;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Phosphatidylcholine synthase;
DE Short=PC synthase;
DE Short=PCS;
DE EC=2.7.8.24;
DE AltName: Full=CDP-diglyceride-choline O-phosphatidyltransferase;
GN Name=pcs; OrderedLocusNames=mll0506;
OS Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS (Mesorhizobium loti (strain MAFF 303099)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=266835;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT Mesorhizobium loti.";
RL DNA Res. 7:331-338(2000).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
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: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:14663079};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000305}.
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DR EMBL; BA000012; BAB48080.1; -; Genomic_DNA.
DR RefSeq; WP_010909436.1; NC_002678.2.
DR AlphaFoldDB; Q98MN3; -.
DR SMR; Q98MN3; -.
DR STRING; 266835.14021468; -.
DR EnsemblBacteria; BAB48080; BAB48080; BAB48080.
DR GeneID; 66684094; -.
DR KEGG; mlo:mll0506; -.
DR eggNOG; COG1183; Bacteria.
DR HOGENOM; CLU_086279_0_0_5; -.
DR OMA; FLHPFRV; -.
DR Proteomes; UP000000552; 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; 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 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..268
FT /note="Phosphatidylcholine synthase"
FT /id="PRO_0000056811"
FT TOPO_DOM 1..27
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 28..48
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 49..53
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..88
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 110..112
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..145
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 167..168
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 190..203
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..240
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 262..268
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 268 AA; 29526 MW; E2C115F15F453A20 CRC64;
MAARKAAKKL TDRIPRPKKK VTWPQARAFS VHLLTASGSF LAFLSLVAAS EERWTAMFWW
LGLALFVDGI DGPIARKLEV KEILPTWSGE LLDNIIDYVT YVLIPAFALY QRGFMGEGLS
FLSAAIIVVS SAIYYADTGM KTKENFFKGF PVVWNMVVFT LFVIEPGQWV SFAVVVVAGI
LTFVPINFIH PVRVVRLRPF NLTMTLLWCA FGALALAQAA LAAFYDQIGV LGAQVSTFIK
IGITITGLYL ACIGGIMQFF PNLGAKKA
