ID   PSSY_CAUVC              Reviewed;         267 AA.
AC   Q9ABR0;
DT   29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=UDP-glucose:undecaprenyl-phosphate glucose-1-phosphate transferase;
DE            Short=UDP-Glc:Und-P Glc-1-P transferase;
DE            EC=2.7.8.31;
DE   AltName: Full=Glucosyl-P-P-undecaprenol synthase;
GN   Name=pssY; OrderedLocusNames=CC_0166;
OS   Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=190650;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19089 / CB15;
RX   PubMed=11259647; DOI=10.1073/pnas.061029298;
RA   Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA   Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA   Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F.,
RA   Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R.,
RA   Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O.,
RA   Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
RT   "Complete genome sequence of Caulobacter crescentus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=ATCC 19089 / CB15;
RX   PubMed=22408159; DOI=10.1128/jb.06052-11;
RA   Patel K.B., Toh E., Fernandez X.B., Hanuszkiewicz A., Hardy G.G.,
RA   Brun Y.V., Bernards M.A., Valvano M.A.;
RT   "Functional characterization of UDP-glucose:undecaprenyl-phosphate glucose-
RT   1-phosphate transferases of Escherichia coli and Caulobacter crescentus.";
RL   J. Bacteriol. 194:2646-2657(2012).
CC   -!- FUNCTION: Is likely the initiating enzyme for holdfast polysaccharide
CC       synthesis. Catalyzes the transfer of the glucose-1-phosphate moiety
CC       from UDP-Glc onto the carrier lipid undecaprenyl phosphate (C55-P),
CC       forming a phosphoanhydride bond yielding to glucosyl-pyrophosphoryl-
CC       undecaprenol (Glc-PP-C55). Also possesses a weak galactose-1-P
CC       transferase activity. {ECO:0000269|PubMed:22408159}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=di-trans,octa-cis-undecaprenyl phosphate + UDP-alpha-D-glucose
CC         = alpha-D-glucosyl di-trans,octa-cis-undecaprenyl diphosphate + UMP;
CC         Xref=Rhea:RHEA:28126, ChEBI:CHEBI:57865, ChEBI:CHEBI:58885,
CC         ChEBI:CHEBI:60392, ChEBI:CHEBI:61254; EC=2.7.8.31;
CC         Evidence={ECO:0000269|PubMed:22408159};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22408159};
CC       Single-pass membrane protein {ECO:0000269|PubMed:22408159}.
CC   -!- MISCELLANEOUS: Complements colanic acid (CA) synthesis in the E.coli
CC       mutant lacking wcaJ. Can also partially complement the O-antigen defect
CC       in the S.typhimurium wbaP deletion strain (PubMed:22408159).
CC       {ECO:0000305|PubMed:22408159}.
CC   -!- SIMILARITY: Belongs to the bacterial sugar transferase family.
CC       {ECO:0000305}.
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DR   EMBL; AE005673; AAK22153.1; -; Genomic_DNA.
DR   PIR; E87269; E87269.
DR   RefSeq; NP_418985.1; NC_002696.2.
DR   AlphaFoldDB; Q9ABR0; -.
DR   SMR; Q9ABR0; -.
DR   STRING; 190650.CC_0166; -.
DR   DNASU; 944218; -.
DR   EnsemblBacteria; AAK22153; AAK22153; CC_0166.
DR   KEGG; ccr:CC_0166; -.
DR   PATRIC; fig|190650.5.peg.163; -.
DR   eggNOG; COG2148; Bacteria.
DR   HOGENOM; CLU_024920_1_2_5; -.
DR   OMA; QVQNIDM; -.
DR   BioCyc; CAULO:CC0166-MON; -.
DR   Proteomes; UP000001816; 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:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR003362; Bact_transf.
DR   Pfam; PF02397; Bac_transf; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Exopolysaccharide synthesis; Glycosyltransferase; Membrane;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..267
FT                   /note="UDP-glucose:undecaprenyl-phosphate glucose-1-
FT                   phosphate transferase"
FT                   /id="PRO_0000422393"
FT   TRANSMEM        83..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   267 AA;  29010 MW;  BFFD221591C24988 CRC64;
     MKEQGLPAVN IIACASPLLC TTTSSDCVSV WACELEQPLS DALGKLKDHP VDLGPSTQLL
     TLRPGGPLPR VAVDLRKRVL DVVAAALLTA LFAPLLLLAA LAIKLESPGP ALFRQTRGGL
     GGAPFQILKL RTMHCREDGP DVAQAQRGDD RVTRVGRILR AASIDELPQL LNVLRGDMSL
     VGPRPHATAH DDYYSARIPE YAARYQARPG LTGLAQVRGL RGGTETVELM RQRIAADIDY
     IQTWSLWRDL KIVLRTVPSL LTTDNAY