ID   GPPUS_KLEPN             Reviewed;         465 AA.
AC   Q48460;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 67.
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=Capsular polysaccharide biosynthesis lipid carrier glucose-1-P transferase;
DE   AltName: Full=Glucosyl-P-P-undecaprenol synthase;
DE   AltName: Full=ORF14;
OS   Klebsiella pneumoniae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Chedid;
RX   PubMed=7896702; DOI=10.1128/jb.177.7.1788-1796.1995;
RA   Arakawa Y., Wacharotayankun R., Nagatsuka T., Ito H., Kato N., Ohta M.;
RT   "Genomic organization of the Klebsiella pneumoniae cps region responsible
RT   for serotype K2 capsular polysaccharide synthesis in the virulent strain
RT   Chedid.";
RL   J. Bacteriol. 177:1788-1796(1995).
CC   -!- FUNCTION: Is likely the initiating enzyme for the K2 capsular
CC       polysaccharide synthesis. Catalyzes the transfer of the glucose-1-
CC       phosphate moiety from UDP-Glc onto the carrier lipid undecaprenyl
CC       phosphate (C55-P), forming a phosphoanhydride bond yielding to
CC       glucosyl-pyrophosphoryl-undecaprenol (Glc-PP-C55) (By similarity).
CC       {ECO:0000250}.
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   -!- PATHWAY: Capsule biogenesis; capsule polysaccharide biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the bacterial sugar transferase family.
CC       {ECO:0000305}.
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DR   EMBL; D21242; BAA04785.1; -; Genomic_DNA.
DR   PIR; C56146; C56146.
DR   AlphaFoldDB; Q48460; -.
DR   SMR; Q48460; -.
DR   UniPathway; UPA00934; -.
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:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR003362; Bact_transf.
DR   InterPro; IPR017475; EPS_sugar_tfrase.
DR   InterPro; IPR017473; Undecaprenyl-P_gluc_Ptfrase.
DR   Pfam; PF02397; Bac_transf; 1.
DR   TIGRFAMs; TIGR03025; EPS_sugtrans; 1.
DR   TIGRFAMs; TIGR03023; WcaJ_sugtrans; 1.
PE   3: Inferred from homology;
KW   Capsule biogenesis/degradation; Cell inner membrane; Cell membrane;
KW   Exopolysaccharide synthesis; Glycosyltransferase;
KW   Lipopolysaccharide biosynthesis; Membrane; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..465
FT                   /note="UDP-glucose:undecaprenyl-phosphate glucose-1-
FT                   phosphate transferase"
FT                   /id="PRO_0000166472"
FT   TRANSMEM        23..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        46..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        82..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        105..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        280..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   465 AA;  53402 MW;  3BFB21503D999482 CRC64;
     MTISQHRFRS NANASIISML QRFSDILIIF LGIYFSCFIN DYFFNLHYVL MALVALVVFQ
     MIGGITDFYR SWRGVEFSVE LILILKNWSL SFLLTLGFVT LFSDFDLTFR TFIFWYLAVC
     AGFVVTRPLI RALAGFFRRI GYNKRRVAFA GSLPAGISLL ETFRKQPWLG FEVKGIYEDS
     FSGTYDLELY AGKISDLINE ARKGTIDRIY IAMHMRDEVA IKNMVSQLTD TTCSVLYIPD
     VFTFNILQSR TEEINGVPVV PLFDSPLNGI NMVFKRLEDI IVSSLILILI SPILLVIATA
     VKTTSKGPVI FRQVRYGMDG KPIKVWKFRS MTVMENDDKV IQATKNDIRV TKVGKFLRST
     SLDELPQFFN VLFGQMSVVG PRPHAVSHNE QYRSLIQGYM LRHKVKPGIT GLAQINGWRG
     ETDTLEKMEK RIEYDLLYIR GWSIWLDLKI IFLTVFKGFI NKSAY