ID   GTRB_SHIFL              Reviewed;         309 AA.
AC   P68667; O21943;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=SfII prophage-derived bactoprenol glucosyl transferase;
DE            EC=2.4.1.-;
GN   Name=gtrB; Synonyms=gtrBI; OrderedLocusNames=SF0306, S0320;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
CC   -!- FUNCTION: Involved in O antigen modification. Catalyzes the transfer of
CC       the glucose residue from UDP-glucose to a lipid carrier (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell 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; AE005674; AAN41965.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP15848.1; -; Genomic_DNA.
DR   RefSeq; NP_706258.1; NC_004337.2.
DR   RefSeq; WP_000703658.1; NZ_QWTR01000152.1.
DR   AlphaFoldDB; P68667; -.
DR   SMR; P68667; -.
DR   STRING; 198214.SF0306; -.
DR   DNASU; 1076753; -.
DR   EnsemblBacteria; AAN41965; AAN41965; SF0306.
DR   EnsemblBacteria; AAP15848; AAP15848; S0320.
DR   GeneID; 1025741; -.
DR   KEGG; sfl:SF0306; -.
DR   KEGG; sft:NCTC1_00323; -.
DR   KEGG; sfx:S0320; -.
DR   PATRIC; fig|198214.7.peg.351; -.
DR   HOGENOM; CLU_033536_0_1_6; -.
DR   OrthoDB; 1064289at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; 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   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   Cell membrane; Glycosyltransferase; Membrane; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..309
FT                   /note="SfII prophage-derived bactoprenol glucosyl
FT                   transferase"
FT                   /id="PRO_0000059191"
FT   TRANSMEM        229..249
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        263..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   309 AA;  34847 MW;  73172FD3AD956014 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 IEVKNRPKYI
     IKKSHRGNP