ID   GTF_ACTP7               Reviewed;         330 AA.
AC   B3H2N1;
DT   01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Alpha-1,6-glucosyltransferase;
DE            Short=alpha6GlcT;
DE            EC=2.4.1.-;
DE   AltName: Full=Polymerizing glucosyltransferase;
GN   OrderedLocusNames=APP7_1696;
OS   Actinobacillus pleuropneumoniae serotype 7 (strain AP76).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=537457;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP76;
RA   Linke B., Buettner F., Martinez-Arias R., Goesmann A., Baltes N.,
RA   Tegetmeyer H., Singh M., Gerlach G.F.;
RT   "Genome and proteome analysis of A. pleuropneumoniae serotype 7.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, PATHWAY, COFACTOR, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=AP76;
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: Catalyzes the transfer of a glucose moiety from UDP-glucose
CC       to another glucose that is N-linked to an asparagine within a peptide
CC       or protein. Can act in a repetitive manner, and this way it elongates
CC       the N-linked glucose by a glycan chain consisting of several alpha-1->6
CC       linked glucose residues. Is able to add up to six glucose units in
CC       vitro. Cannot use UDP-Gal, UDP-GlcNAc or UDP-GalNAc as a substrate
CC       donor. {ECO:0000269|PubMed:21852240}.
CC   -!- COFACTOR:
CC       Note=Does not require a metal cofactor. {ECO:0000269|PubMed:21852240};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000269|PubMed:21852240}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:21852240}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC       {ECO:0000305}.
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DR   EMBL; CP001091; ACE62348.1; -; Genomic_DNA.
DR   RefSeq; WP_005618105.1; NC_010939.1.
DR   AlphaFoldDB; B3H2N1; -.
DR   SMR; B3H2N1; -.
DR   EnsemblBacteria; ACE62348; ACE62348; APP7_1696.
DR   KEGG; apa:APP7_1696; -.
DR   HOGENOM; CLU_840997_0_0_6; -.
DR   OMA; FPRMIMH; -.
DR   BioCyc; APLE537457:APP7_RS08795-MON; -.
DR   UniPathway; UPA00378; -.
DR   PHI-base; PHI:6866; -.
DR   Proteomes; UP000001226; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0035251; F:UDP-glucosyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   Cytoplasm; Glycosyltransferase; Transferase.
FT   CHAIN           1..330
FT                   /note="Alpha-1,6-glucosyltransferase"
FT                   /id="PRO_0000430339"
SQ   SEQUENCE   330 AA;  38069 MW;  44BC32A51330C99C CRC64;
     MENNIDLNVY FCFVNRPCTG GDFVNLDHVR TLRKLGINAS ILLAGNQSEE IVNSFGSLPV
     VILNEEIEFS SQDIFIVPEV MQVLYDLASK MTVFPRMIMH NQNPFYTGYG FLSAQHINEH
     RLERIIVPSS YTKYKLQEIG VTKPIDIIHP YIPDYFKPAE KQREVIQIAF SRRKRSAEFD
     IFKFYFLSLY SHKHSVNFVN IQGLTREEVA KVMSEAAIFI SFAERESLGL MTLEAMASGC
     HVIGFSGYTD IYNNEVIDDS VGDWIGEGEY TLFAQKVCQA IDDFVNGKMN PKIENGLRLI
     EQRFRIRHFE QEVKRVYGNI FDYDLENSRS