ID   NGT_ACTP2               Reviewed;         620 AA.
AC   A3N2T3;
DT   01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=UDP-glucose:protein N-beta-glucosyltransferase;
DE            Short=UDP-Glc:protein N-glucosyltransferase;
DE            EC=2.4.1.-;
DE   AltName: Full=HMW1C-like protein;
DE   AltName: Full=N-glycosyltransferase;
DE            Short=NGT;
GN   OrderedLocusNames=APL_1635;
OS   Actinobacillus pleuropneumoniae serotype 5b (strain L20).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=416269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L20;
RX   PubMed=18065534; DOI=10.1128/jb.01845-07;
RA   Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M.,
RA   Nash J.H.E.;
RT   "The complete genome sequence of Actinobacillus pleuropneumoniae L20
RT   (serotype 5b).";
RL   J. Bacteriol. 190:1495-1496(2008).
RN   [2]
RP   FUNCTION AS A GLUCOSYLTRANSFERASE.
RC   STRAIN=L20;
RX   PubMed=21852240; DOI=10.1074/jbc.m111.277160;
RA   Schwarz F., Fan Y.Y., Schubert M., Aebi M.;
RT   "Cytoplasmic N-glycosyltransferase of Actinobacillus pleuropneumoniae is an
RT   inverting enzyme and recognizes the NX(S/T) consensus sequence.";
RL   J. Biol. Chem. 286:35267-35274(2011).
CC   -!- FUNCTION: Inverting glycosyltransferase that catalyzes the transfer of
CC       one glucose moiety from UDP-glucose to an asparagine residue in
CC       peptides and proteins containing the NX(S/T) motif, resulting in their
CC       modification with a beta-linked 1,N-glucose. Likely acts as a key
CC       component of a general protein glycosylation system (Probable).
CC       {ECO:0000305|PubMed:21852240}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-asparaginyl-[protein] + UDP-alpha-D-glucose = H(+) + N(4)-
CC         (beta-D-glucosyl)-L-asparaginyl-[protein] + UDP;
CC         Xref=Rhea:RHEA:45952, Rhea:RHEA-COMP:11400, Rhea:RHEA-COMP:12804,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:50347, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:58885, ChEBI:CHEBI:85501;
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 41 family.
CC       {ECO:0000305}.
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DR   EMBL; CP000569; ABN74719.1; -; Genomic_DNA.
DR   RefSeq; WP_005605627.1; NC_009053.1.
DR   AlphaFoldDB; A3N2T3; -.
DR   SMR; A3N2T3; -.
DR   STRING; 416269.APL_1635; -.
DR   CAZy; GT41; Glycosyltransferase Family 41.
DR   EnsemblBacteria; ABN74719; ABN74719; APL_1635.
DR   KEGG; apl:APL_1635; -.
DR   eggNOG; COG3914; Bacteria.
DR   HOGENOM; CLU_441347_0_0_6; -.
DR   OMA; MKLNPYF; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000001432; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR040542; HMW1_D2.
DR   InterPro; IPR041109; HMW1C_N.
DR   Pfam; PF18254; HMw1_D2; 1.
DR   Pfam; PF18071; HMW1C_N; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Glycosyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..620
FT                   /note="UDP-glucose:protein N-beta-glucosyltransferase"
FT                   /id="PRO_0000430338"
SQ   SEQUENCE   620 AA;  70494 MW;  3AC72D008708BC7D CRC64;
     MENENKPNVA NFEAAVAAKD YEKACSELLL ILSQLDSNFG GIHEIEFEYP AQLQDLEQEK
     IVYFCTRMAT AITTLFSDPV LEISDLGVQR FLVYQRWLAL IFASSPFVNA DHILQTYNRE
     PNRKNSLEIH LDSSKSSLIK FCILYLPESN VNLNLDVMWN ISPELCASLC FALQSPRFVG
     TSTAFNKRAT ILQWFPRHLD QLKNLNNIPS AISHDVYMHC SYDTSVNKHD VKRALNHVIR
     RHIESEYGWK DRDVAHIGYR NNKPVMVVLL EHFHSAHSIY RTHSTSMIAA REHFYLIGLG
     SPSVDQAGQE VFDEFHLVAG DNMKQKLEFI RSVCESNGAA IFYMPSIGMD MTTIFASNTR
     LAPIQAIALG HPATTHSDFI EYVIVEDDYV GSEECFSETL LRLPKDALPY VPSALAPEKV
     DYLLRENPEV VNIGIASTTM KLNPYFLEAL KAIRDRAKVK VHFHFALGQS NGITHPYVER
     FIKSYLGDSA TAHPHSPYHQ YLRILHNCDM MVNPFPFGNT NGIIDMVTLG LVGVCKTGAE
     VHEHIDEGLF KRLGLPEWLI ANTVDEYVER AVRLAENHQE RLELRRYIIE NNGLNTLFTG
     DPRPMGQVFL EKLNAFLKEN