ID   GTRB_BPSF5              Reviewed;         307 AA.
AC   O22007;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   29-SEP-2021, entry version 82.
DE   RecName: Full=Bactoprenol glucosyl transferase;
DE            EC=2.4.1.-;
GN   Name=gtrB; Synonyms=24;
OS   Shigella phage SfV (Shigella flexneri bacteriophage V) (Bacteriophage SfV).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Myoviridae.
OX   NCBI_TaxID=55884;
OH   NCBI_TaxID=623; Shigella flexneri.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9305766; DOI=10.1016/s0378-1119(97)00144-3;
RA   Huan P.T., Whittle B.L., Bastin D.A., Lindberg A.A., Verma N.K.;
RT   "Shigella flexneri type-specific antigen V: cloning, sequencing and
RT   characterization of the glucosyl transferase gene of temperate
RT   bacteriophage SfV.";
RL   Gene 195:207-216(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11889106; DOI=10.1128/jb.184.7.1974-1987.2002;
RA   Allison G.E., Angeles D., Tran-Dinh N., Verma N.K.;
RT   "Complete genomic sequence of SfV, a serotype-converting temperate
RT   bacteriophage of Shigella flexneri.";
RL   J. Bacteriol. 184:1974-1987(2002).
CC   -!- FUNCTION: Involved in O antigen modification. Catalyzes the transfer of
CC       the glucose residue from UDP-glucose to a lipid carrier.
CC   -!- SUBCELLULAR LOCATION: Host membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GtrB
CC       subfamily. {ECO:0000305}.
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DR   EMBL; U82619; AAB72133.1; -; Genomic_DNA.
DR   RefSeq; NP_599056.1; NC_003444.1.
DR   SMR; O22007; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   GeneID; 935195; -.
DR   KEGG; vg:935195; -.
DR   Proteomes; UP000009068; Genome.
DR   GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR001173; Glyco_trans_2-like.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   Pfam; PF00535; Glycos_transf_2; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Host membrane; Membrane; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..307
FT                   /note="Bactoprenol glucosyl transferase"
FT                   /id="PRO_0000059192"
FT   TRANSMEM        229..249
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        263..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   307 AA;  34708 MW;  54917F5BC0FA031A CRC64;
     MKISLVVPVF NEEEAIPVFY KTVREFQELK PYEVEIVFIN DGSKDATESI INALAVSDPL
     VVPLSFTRNF GKEPALFAGL DHASGDAVIP IDVDLQDPIE VIPHLIEKWQ AGADMVLAKR
     SDRSTDGRLK RKTAEWFYKL HNKISTPKIE ENVGDFRLMS REVVENIKLL PERNLFMKGI
     LSWVGGQTDV VEYVRAERVA GISKFNGWKL WNLALEGITS FSTFPLRVWT YIGLFVASIS
     FLYGAWMIID TLVFGNPVRG YPSLLVSILF LGGVQLIGIG VLGEYIGRIY IESKHRPKYI
     IKNEKQK