PCS_AGRFC
ID PCS_AGRFC Reviewed; 241 AA.
AC A9CIM3;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Phosphatidylcholine synthase {ECO:0000303|PubMed:14663079, ECO:0000312|EMBL:AAK87563.2};
DE Short=PC synthase {ECO:0000303|PubMed:17010159, ECO:0000303|PubMed:18978052};
DE Short=PCS {ECO:0000303|PubMed:14663079, ECO:0000303|PubMed:17010159, ECO:0000303|PubMed:18978052};
DE EC=2.7.8.24 {ECO:0000269|PubMed:14663079, ECO:0000269|PubMed:17010159, ECO:0000269|PubMed:18978052};
DE AltName: Full=CDP-diglyceride-choline O-phosphatidyltransferase {ECO:0000250|UniProtKB:Q9KJY8};
GN Name=pcs {ECO:0000312|EMBL:AAK87563.2}; OrderedLocusNames=Atu1793;
OS Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS (strain C58)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=176299;
RN [1] {ECO:0000312|EMBL:AAK87563.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743193; DOI=10.1126/science.1066804;
RA Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y.,
RA Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P.,
RA Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F.,
RA Gordon M.P., Olson M.V., Nester E.W.;
RT "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT C58.";
RL Science 294:2317-2323(2001).
RN [2] {ECO:0000312|EMBL:AAK87563.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743194; DOI=10.1126/science.1066803;
RA Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT "Genome sequence of the plant pathogen and biotechnology agent
RT Agrobacterium tumefaciens C58.";
RL Science 294:2323-2328(2001).
RN [3] {ECO:0000305}
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=C58 / ATCC 33970 {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 [4] {ECO:0000305}
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=C58 / ATCC 33970 {ECO:0000269|PubMed:17010159};
RX PubMed=17010159; DOI=10.1111/j.1365-2958.2006.05425.x;
RA Wessel M., Klusener S., Godeke J., Fritz C., Hacker S., Narberhaus F.;
RT "Virulence of Agrobacterium tumefaciens requires phosphatidylcholine in the
RT bacterial membrane.";
RL Mol. Microbiol. 62:906-915(2006).
RN [5] {ECO:0000305}
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=C58 / ATCC 33970 {ECO:0000269|PubMed:18978052};
RX PubMed=18978052; DOI=10.1128/jb.01183-08;
RA Klusener S., Aktas M., Thormann K.M., Wessel M., Narberhaus F.;
RT "Expression and physiological relevance of Agrobacterium tumefaciens
RT phosphatidylcholine biosynthesis genes.";
RL J. Bacteriol. 191:365-374(2009).
CC -!- FUNCTION: Condenses choline with CDP-diglyceride to produce
CC phosphatidylcholine and CMP. Affects motility, biofilm formation and
CC virulence of this bacterium when there is a complete loss of
CC phosphatidylcholine formation due to absence of both the synthase (pcs)
CC and the methylation (pmtA) pathways. {ECO:0000269|PubMed:14663079,
CC ECO:0000269|PubMed:17010159, ECO:0000269|PubMed:18978052}.
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:17010159,
CC ECO:0000269|PubMed:18978052};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9KJY8};
CC -!- INTERACTION:
CC A9CIM3; A9CIM3: pcs; NbExp=3; IntAct=EBI-9549403, EBI-9549403;
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; AE007869; AAK87563.2; -; Genomic_DNA.
DR RefSeq; NP_354778.2; NC_003062.2.
DR RefSeq; WP_010971870.1; NC_003062.2.
DR AlphaFoldDB; A9CIM3; -.
DR SMR; A9CIM3; -.
DR MINT; A9CIM3; -.
DR STRING; 176299.Atu1793; -.
DR EnsemblBacteria; AAK87563; AAK87563; Atu1793.
DR KEGG; atu:Atu1793; -.
DR PATRIC; fig|176299.10.peg.1809; -.
DR eggNOG; COG1183; Bacteria.
DR HOGENOM; CLU_086279_0_0_5; -.
DR OMA; FLHPFRV; -.
DR PhylomeDB; A9CIM3; -.
DR BRENDA; 2.7.8.24; 200.
DR PRO; PR:A9CIM3; -.
DR Proteomes; UP000000813; Chromosome circular.
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:0042802; F:identical protein binding; IPI:IntAct.
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..241
FT /note="Phosphatidylcholine synthase"
FT /id="PRO_0000425216"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9KJY8, ECO:0000255"
FT TRANSMEM 16..36
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..41
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..76
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..100
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..133
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 155..159
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..187
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..214
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..235
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..241
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9KJY8, ECO:0000255"
SQ SEQUENCE 241 AA; 26756 MW; 8FAA1B16FD7CC00E CRC64;
MKIFNYKRVP YAEIRAFSVH ILTASGSFLA FLGVVAASEH RFVDMFWWLG LALLVDGIDG
PIARKVRVKE VLPNWSGDTL DNIIDYVTYV LLPAFALYQS GMIGEPLSFV AAGMIVVSSA
IYYADMGMKT DEYFFSGFPV VWNMVVFTLF VMDASATTAM TVVTVSVFLT FLPINFLHPV
RVKRLRPLNL LVVAIWCALG GYALLMHFET PTWAVIAFVA SGIYLYCIGG ILQFFPSLGA
K
