PCS_BRUME
ID PCS_BRUME Reviewed; 276 AA.
AC D0B707; Q8YC37;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Phosphatidylcholine synthase {ECO:0000303|PubMed:14663079, ECO:0000312|EMBL:AAL53937.1};
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:0000312|EMBL:AAL53937.1};
DE AltName: Full=CDP-diglyceride-choline O-phosphatidyltransferase {ECO:0000250|UniProtKB:Q9KJY8, ECO:0000312|EMBL:EEW87399.1};
GN Name=pcs {ECO:0000250|UniProtKB:Q9KJY8}; OrderedLocusNames=BMEII0695;
GN ORFNames=BAWG_1878;
OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=224914;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16M / ATCC 23456 / NCTC 10094;
RX PubMed=11756688; DOI=10.1073/pnas.221575398;
RA DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA Haselkorn R., Kyrpides N.C., Overbeek R.;
RT "The genome sequence of the facultative intracellular pathogen Brucella
RT melitensis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
RN [2] {ECO:0000312|EMBL:EEW87399.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16M / ATCC 23456 / NCTC 10094 {ECO:0000312|EMBL:EEW87399.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L.,
RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T.,
RA White J., Yandava C., Whatmore A.M., Perrett L.L., O'Callaghan D.,
RA Nusbaum C., Galagan J., Birren B.;
RT "The genome sequence of Brucella melitensis bv. 1 str. 16M.";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=16M / ATCC 23456 / NCTC 10094 {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: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;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL53937.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE008918; AAL53937.1; ALT_INIT; Genomic_DNA.
DR EMBL; GG703779; EEW87399.1; -; Genomic_DNA.
DR PIR; AF3596; AF3596.
DR RefSeq; WP_004686877.1; NZ_GG703779.1.
DR AlphaFoldDB; D0B707; -.
DR SMR; D0B707; -.
DR STRING; 224914.BMEII0695; -.
DR EnsemblBacteria; AAL53937; AAL53937; BMEII0695.
DR GeneID; 45125922; -.
DR KEGG; bme:BMEII0695; -.
DR eggNOG; COG1183; Bacteria.
DR PhylomeDB; D0B707; -.
DR BRENDA; 2.7.8.24; 995.
DR Proteomes; UP000000419; Chromosome II.
DR Proteomes; UP000008511; Unassembled WGS sequence.
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 Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..276
FT /note="Phosphatidylcholine synthase"
FT /id="PRO_0000425219"
FT TOPO_DOM 1..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9KJY8, ECO:0000255"
FT TRANSMEM 31..51
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..57
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..91
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..115
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..146
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 168..171
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..202
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..230
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 252..276
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9KJY8, ECO:0000255"
SQ SEQUENCE 276 AA; 30442 MW; 26042E4A70A4C359 CRC64;
MGGQKEMADS VKTKLTGKLK AKKVTAPQAK AFSVHLLTAS GSFLAFLSVV AASDGRYTAM
WWWLGLALFV DGIDGPIARK LEVKYVLPNW SGELLDSIID YVTYVLIPAF ALYQSGFMGT
NLSFISGAII VVSSAIYYAD TGMKTKENFF KGFPVVWNMV VFTLFIVRPG EWVAFGTVVA
SAILSFLPIN FLHPVRVVRL RPLNLTIFLL WCAFGVIALY YMLDAPLWVR IGISVTGLYI
YFIGAIMQLF PSLGREAALA KARKLVEKQQ KSGEAP
