ID   GTF3_LIMR1              Reviewed;         334 AA.
AC   B3XPQ7;
DT   08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 25.
DE   RecName: Full=Glucosyltransferase 3 {ECO:0000255|HAMAP-Rule:MF_00841};
DE            EC=2.4.1.- {ECO:0000255|HAMAP-Rule:MF_00841, ECO:0000305|PubMed:30371779};
GN   Name=gtf3 {ECO:0000255|HAMAP-Rule:MF_00841};
GN   Synonyms=gtfC {ECO:0000303|PubMed:30371779}; ORFNames=Lreu23DRAFT_5181;
OS   Limosilactobacillus reuteri (strain DSM 17509 / CIP 109821 / 100-23)
OS   (Lactobacillus reuteri).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Limosilactobacillus.
OX   NCBI_TaxID=349123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17509 / CIP 109821 / 100-23;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Sun H., Schmutz J., Larimer F., Land M., Hauser L., Walter J., Heng N.C.K.,
RA   Tannock G.W., Richardson P.;
RT   "Permanent draft sequence of Lactobacillus reuteri 100-23.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, AND PATHWAY.
RC   STRAIN=DSM 17509 / CIP 109821 / 100-23;
RX   PubMed=30371779; DOI=10.1093/glycob/cwy100;
RA   Latousakis D., Nepravishta R., Rejzek M., Wegmann U., Le Gall G.,
RA   Kavanaugh D., Colquhoun I.J., Frese S., MacKenzie D.A., Walter J.,
RA   Angulo J., Field R.A., Juge N.;
RT   "Serine-rich repeat protein adhesins from Lactobacillus reuteri display
RT   strain specific glycosylation profiles.";
RL   Glycobiology 29:45-58(2019).
CC   -!- FUNCTION: Required for polymorphic O-glycosylation of the serine-rich
CC       repeat protein in this bacteria. Catalyzes the second step in
CC       glycosylation by transferring glucose from UDP-glucose to the terminal
CC       GlcNAc moiety of the 3-O-(N-acetyl-alpha-D-glucosaminyl)-L-seryl-
CC       [protein] resulting from the first glycosylation step.
CC       {ECO:0000269|PubMed:30371779}.
CC   -!- FUNCTION: Part of the accessory SecA2/SecY2 system specifically
CC       required to export serine-rich repeat cell wall protein(s) encoded
CC       upstream in the same operon. {ECO:0000305|PubMed:30371779}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000255|HAMAP-Rule:MF_00841, ECO:0000269|PubMed:30371779}.
CC   -!- SUBUNIT: Homotetramer; a dimer of dimers. {ECO:0000255|HAMAP-
CC       Rule:MF_00841}.
CC   -!- DOMAIN: Dimerizes via the C-terminus; dimerization is required for
CC       tetramer formation. Binds protein substrate via an exposed loop in the
CC       N-terminus. {ECO:0000255|HAMAP-Rule:MF_00841}.
CC   -!- MISCELLANEOUS: L.reuteri is generally considered to be a symbiont
CC       rather than pathogenic bacteria. This strain was isolated from rat.
CC       {ECO:0000305|PubMed:30371779}.
CC   -!- SIMILARITY: Belongs to the Gtf3 glucosyltransferase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00841}.
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; AAPZ02000001; EDX43653.1; -; Genomic_DNA.
DR   RefSeq; WP_003665713.1; NZ_AAPZ02000001.1.
DR   AlphaFoldDB; B3XPQ7; -.
DR   SMR; B3XPQ7; -.
DR   STRING; 349123.Lreu23DRAFT_5181; -.
DR   EnsemblBacteria; EDX43653; EDX43653; Lreu23DRAFT_5181.
DR   PATRIC; fig|349123.13.peg.2203; -.
DR   eggNOG; COG0438; Bacteria.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000003853; Unassembled WGS sequence.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0035251; F:UDP-glucosyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_00841; Gtf3; 1.
DR   InterPro; IPR043676; Gtf3.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Nucleotide-binding; Transferase.
FT   CHAIN           1..334
FT                   /note="Glucosyltransferase 3"
FT                   /id="PRO_0000447234"
FT   BINDING         16
FT                   /ligand="UDP"
FT                   /ligand_id="ChEBI:CHEBI:58223"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00841"
FT   BINDING         180
FT                   /ligand="UDP"
FT                   /ligand_id="ChEBI:CHEBI:58223"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00841"
FT   BINDING         249..254
FT                   /ligand="UDP"
FT                   /ligand_id="ChEBI:CHEBI:58223"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00841"
SQ   SEQUENCE   334 AA;  38194 MW;  5DBE1264BE834A05 CRC64;
     MTVHITNLYG QSFQSTAQIA QNQIAKIGRE LGFNELGIYS YNWPDEPSVA LDTRFDGIIA
     SVSNNDTVIF QSPTWNSIEW DQAFIDHLAP YNVKKIIFIH DIIPLMFESN RYLLPQFIDY
     YNKADLIIAP SQPMVDFLRA NGLTVEKVVL QHMWDHYASV DFTVTPQNTG VINLAGNLEK
     FQLVGHWHYP NNPLYAFAKV IDIEPTDNIK FMGWQSDPVL LSKLRHNGGF GLVWSNESYW
     KNYMHLNANH KLSTYLAAGL PVIVNENIAE SETILRKGLG IVADNLDEAI EKVQGMDDQS
     YNEMVQRVDD FARLIREGYF AKKALTEAVF NLYY