GTRB_BPSF2
ID GTRB_BPSF2 Reviewed; 309 AA.
AC P68668; O21943;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 29-SEP-2021, entry version 47.
DE RecName: Full=Bactoprenol glucosyl transferase;
DE EC=2.4.1.-;
GN Name=gtrB; Synonyms=bgt;
OS Shigella phage SfII (Shigella flexneri bacteriophage II) (Bacteriophage
OS SfII).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae.
OX NCBI_TaxID=66284;
OH NCBI_TaxID=623; Shigella flexneri.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9426131; DOI=10.1046/j.1365-2958.1997.6301997.x;
RA Mavris M., Manning P.A., Morona R.;
RT "Mechanism of bacteriophage SfII-mediated serotype conversion in Shigella
RT flexneri.";
RL Mol. Microbiol. 26:939-950(1997).
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: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GtrB
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF021347; AAC39272.1; -; Genomic_DNA.
DR RefSeq; YP_008318506.1; NC_021857.1.
DR SMR; P68668; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR GeneID; 16384913; -.
DR KEGG; vg:16384913; -.
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; Membrane; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..309
FT /note="Bactoprenol glucosyl transferase"
FT /id="PRO_0000059190"
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