ID   GTF3_LIMR5              Reviewed;         340 AA.
AC   F8KEJ1;
DT   08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 1.
DT   03-AUG-2022, entry version 22.
DE   RecName: Full=N-acetylglucosaminyltransferase {ECO:0000305|PubMed:30371779};
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=LRATCC53608_1104;
OS   Limosilactobacillus reuteri (strain ATCC 53608) (Lactobacillus reuteri).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Limosilactobacillus.
OX   NCBI_TaxID=927703;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 53608;
RX   PubMed=21622738; DOI=10.1128/jb.05282-11;
RA   Heavens D., Tailford L.E., Crossman L., Jeffers F., Mackenzie D.A.,
RA   Caccamo M., Juge N.;
RT   "Genome sequence of the vertebrate gut symbiont Lactobacillus reuteri ATCC
RT   53608.";
RL   J. Bacteriol. 193:4015-4016(2011).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC   STRAIN=ATCC 53608;
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 N-acetylglucosamine from UDP-GlcNAc to
CC       the terminal GlcNAc moiety of the 3-O-(N-acetyl-alpha-D-glucosaminyl)-
CC       L-seryl-[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   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-O-[N-acetyl-alpha-D-glucosaminyl]-L-seryl-[protein] + UDP-N-
CC         acetyl-alpha-D-glucosamine = 3-O-[N-acetyl-beta-D-glucosaminyl-
CC         (1->6)-N-acetyl-alpha-D-glucosaminyl]-L-seryl-[protein] + H(+) + UDP;
CC         Xref=Rhea:RHEA:59860, Rhea:RHEA-COMP:15466, Rhea:RHEA-COMP:15471,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:143272, ChEBI:CHEBI:143279;
CC         Evidence={ECO:0000269|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 pig.
CC       {ECO:0000305|PubMed:30371779}.
CC   -!- SIMILARITY: Belongs to the Gtf3 glucosyltransferase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00841}.
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DR   EMBL; FR854365; CCC03856.1; -; Genomic_DNA.
DR   AlphaFoldDB; F8KEJ1; -.
DR   SMR; F8KEJ1; -.
DR   HOGENOM; CLU_057651_0_0_9; -.
DR   UniPathway; UPA00378; -.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0035251; F:UDP-glucosyltransferase activity; IEA:InterPro.
DR   GO; GO:0008194; F:UDP-glycosyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_00841; Gtf3; 1.
DR   InterPro; IPR043676; Gtf3.
PE   1: Evidence at protein level;
KW   Glycosyltransferase; Nucleotide-binding; Transferase.
FT   CHAIN           1..340
FT                   /note="N-acetylglucosaminyltransferase"
FT                   /id="PRO_0000447235"
FT   BINDING         21
FT                   /ligand="UDP"
FT                   /ligand_id="ChEBI:CHEBI:58223"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00841"
FT   BINDING         185
FT                   /ligand="UDP"
FT                   /ligand_id="ChEBI:CHEBI:58223"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00841"
FT   BINDING         254..259
FT                   /ligand="UDP"
FT                   /ligand_id="ChEBI:CHEBI:58223"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00841"
SQ   SEQUENCE   340 AA;  38767 MW;  547BEAC8B6C4BF06 CRC64;
     MEGLSLTVHI TNLYGQSFQS TAQIAQNQIA KIGRELGFNE LGIYNYNWPD EPSVALDTRF
     DGIIASVSNN DTVIFQSPTW NSIEWDQAFI DHLAPYNVKK IIFIHDIIPL MFESNRYLLP
     QFIDYYNKAD LIIAPSQPMV DFLRANGLTV EKVVLQHMWD HCASVDFTVT LQNTGVINFA
     GNLEKFQLVG HWHYPDNPLY AFAKVIDVEP TDNIKFMGWQ SDPVLLSKLR HNGGFGLVWS
     NEPYCKNYMH LNANHKLSTY LAAGLPVIVN ENIAESETIL RKGLGIVADN LDEAIEKVQG
     MDDQSYNEMV QRVDDFARLI REGYFAKKAL TEAVFKLYYQ