ID   GUMD_XANCE              Reviewed;         484 AA.
AC   Q56770;
DT   29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 57.
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=gumD;
OS   Xanthomonas campestris pv. campestris.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=340;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 13951 / NCIB 11803 / NRRL B-1459;
RA   Capage M.A., Doherty D.H., Betlach M.R., Vanderslice R.W.;
RT   "Recombinant-DNA mediated production of xanthan gum.";
RL   Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION IN XANTHAN BIOSYNTHESIS, DISRUPTION PHENOTYPE, PATHWAY, AND
RP   DOMAIN.
RC   STRAIN=ATCC 13951 / NCIB 11803 / NRRL B-1459;
RX   PubMed=9537354; DOI=10.1128/jb.180.7.1607-1617.1998;
RA   Katzen F., Ferreiro D.U., Oddo C.G., Ielmini M.V., Becker A., Puhler A.,
RA   Ielpi L.;
RT   "Xanthomonas campestris pv. campestris gum mutants: effects on xanthan
RT   biosynthesis and plant virulence.";
RL   J. Bacteriol. 180:1607-1617(1998).
CC   -!- FUNCTION: Is the initiating enzyme for the synthesis of the
CC       exopolysaccharide xanthan. 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).
CC       {ECO:0000269|PubMed:9537354}.
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: Glycan biosynthesis; xanthan biosynthesis.
CC       {ECO:0000269|PubMed:9537354}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- DOMAIN: The C-terminal domain is sufficient for glucosyl-1-phosphate
CC       transferase activity. {ECO:0000269|PubMed:9537354}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene fail to synthesize any
CC       xanthan biosynthetic lipid sugar intermediates. They do not produce
CC       xanthan and exhibit a 50% virulence index reduction.
CC       {ECO:0000269|PubMed:9537354}.
CC   -!- SIMILARITY: Belongs to the bacterial sugar transferase family.
CC       {ECO:0000305}.
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DR   EMBL; U22511; AAA86372.1; -; Genomic_DNA.
DR   PIR; S67820; S67820.
DR   RefSeq; WP_057672146.1; NZ_CDNB01000028.1.
DR   AlphaFoldDB; Q56770; -.
DR   SMR; Q56770; -.
DR   BioCyc; MetaCyc:MON-15979; -.
DR   UniPathway; UPA01017; -.
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:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000271; P:polysaccharide 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   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Exopolysaccharide synthesis; Membrane;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..484
FT                   /note="UDP-glucose:undecaprenyl-phosphate glucose-1-
FT                   phosphate transferase"
FT                   /id="PRO_0000422392"
FT   TRANSMEM        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        59..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        93..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        122..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        299..319
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   484 AA;  54636 MW;  88E41F3BCD681290 CRC64;
     MLLADLSSAT YTTSSPRLLS KYSAAADLVL RVFDLTMVVA SGLIAYRIVF GTWVPAAPYR
     VAIATTLLYS VICFALFPLY RSWRGRGLLS ELVVLGGAFG GVFALFAVHA LIVQVGEQVS
     RGWVGLWFVG GLVSLVAART LLRGFLNHLR TQGVDVQRVV VVGLRHPVMK ISHYLSRNPW
     VGMNMVGYFR TPYDLAVAEQ RQGLPCLGDP DELIEYLKNN QVEQVWISLP LGERDHIKQL
     LQRLDRYPIN VKLVPDLFDF GLLNQSAEQI GSVPVINLRQ GGVDRDNYFV VAKALQDKIL
     AVIALMGLWP LMLAIAVGVK MSSPGPVFFR QRRHGLGGRE FYMFKFRSMR VHDDHGTTIQ
     QATKNDTRIT RFGSFLRRSS LDELPQIFNV LGGSMSIVGP RPHAAQHNTH YEKLINHYMQ
     RHYVKPGITG WAQVNGFRGE TPELRTMKKR IQYDLDYIRR WSLWLDIRII VLTAVRVLGQ
     KTAY