ID   GUMI_XANCP              Reviewed;         349 AA.
AC   Q8P804;
DT   16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=GDP-mannose:glycolipid 4-beta-D-mannosyltransferase;
DE            EC=2.4.1.251;
DE   AltName: Full=GlcA-beta-(1->2)-D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphoundecaprenol 4-beta-mannosyltransferase;
DE   Flags: Precursor;
GN   Name=gumI; OrderedLocusNames=XCC2447;
OS   Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS   528 / LMG 568 / P 25).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA   Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA   Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA   Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA   Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA   Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA   Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA   Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA   Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA   Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA   Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA   Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA   Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT   specificities.";
RL   Nature 417:459-463(2002).
CC   -!- FUNCTION: Nonprocessive beta-mannosyltransferase that catalyzes the
CC       transfer of a mannose residue from GDP-mannose to glucuronic acid-beta-
CC       1,2-mannose-alpha-1,3-glucose-beta-1,4-glucose-PP-polyisoprenyl to form
CC       the lipid-linked pentasaccharide repeating unit of xanthan, Man-GlcA-
CC       Man-Glc(2)-PP-Pol. Is involved in the biosynthesis of the
CC       exopolysaccharide xanthan (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-GlcA-(1->2)-alpha-D-Man-(1->3)-beta-D-Glc-(1->4)-alpha-
CC         D-Glc-di-trans,octa-cis-undecaprenyl diphosphate + GDP-alpha-D-
CC         mannose = beta-D-Man-(1->4)-beta-D-GlcA-(1->2)-alpha-D-Man-(1->3)-
CC         beta-D-Glc-(1->4)-alpha-D-Glc-di-trans,octa-cis-undecaprenyl
CC         diphosphate + GDP + H(+); Xref=Rhea:RHEA:28306, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57527, ChEBI:CHEBI:58189, ChEBI:CHEBI:61227,
CC         ChEBI:CHEBI:61230; EC=2.4.1.251;
CC   -!- PATHWAY: Glycan biosynthesis; xanthan biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 94 family.
CC       {ECO:0000305}.
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DR   EMBL; AE008922; AAM41724.1; -; Genomic_DNA.
DR   RefSeq; NP_637800.1; NC_003902.1.
DR   RefSeq; WP_011037588.1; NC_003902.1.
DR   AlphaFoldDB; Q8P804; -.
DR   SMR; Q8P804; -.
DR   STRING; 340.xcc-b100_1719; -.
DR   CAZy; GT94; Glycosyltransferase Family 94.
DR   EnsemblBacteria; AAM41724; AAM41724; XCC2447.
DR   KEGG; xcc:XCC2447; -.
DR   PATRIC; fig|190485.4.peg.2611; -.
DR   eggNOG; COG0438; Bacteria.
DR   HOGENOM; CLU_009583_6_0_6; -.
DR   OMA; IPHGHYR; -.
DR   UniPathway; UPA01017; -.
DR   PHI-base; PHI:6665; -.
DR   Proteomes; UP000001010; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cell inner membrane; Cell membrane;
KW   Glycosyltransferase; Membrane; Reference proteome; Signal; Transferase.
FT   SIGNAL          1..14
FT                   /evidence="ECO:0000255"
FT   CHAIN           15..349
FT                   /note="GDP-mannose:glycolipid 4-beta-D-mannosyltransferase"
FT                   /id="PRO_0000414018"
SQ   SEQUENCE   349 AA;  39076 MW;  7F8779B341750E52 CRC64;
     MSASASLPVT RAAAAPRITV LFSTEKPNAN TNPYLTQLYD ALPDAVQPRF FSMREALLSR
     YDVLHLHWPE YLLRHPSKMG TLAKQACAAL LLMKLQLTGT PVVRTLHNLA PHEDRGWRER
     ALLRWIDQLT RRWIRINATT PVRPPFTDTI LHGHYRDWFA TMEQGTTVPG RLLHFGLIRP
     YKGVEVLLDV MRDVQDPRLS LRIVGNPATP QMRTLVETAC AQDARISALL AYVEEPVLAR
     EVSACELVVL PYKQMHNSGT LLLALSLARP VLAPWSESNA AIAEEVGPGW VFLYEGEFDA
     ALLSGMLDQV RAAPRGPAPD LSQRDWPRIG QLHYRTYLEA LGKDGDAAL