PGLI_CAMJE
ID PGLI_CAMJE Reviewed; 309 AA.
AC Q0P9C6;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=GalNAc(5)-diNAcBac-PP-undecaprenol beta-1,3-glucosyltransferase;
DE EC=2.4.1.293;
DE AltName: Full=Protein glycosylation I;
GN Name=pglI; OrderedLocusNames=Cj1128c;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=16186480; DOI=10.1073/pnas.0507311102;
RA Glover K.J., Weerapana E., Imperiali B.;
RT "In vitro assembly of the undecaprenylpyrophosphate-linked heptasaccharide
RT for prokaryotic N-linked glycosylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:14255-14259(2005).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=16547029; DOI=10.1128/jb.188.7.2427-2434.2006;
RA Kelly J., Jarrell H., Millar L., Tessier L., Fiori L.M., Lau P.C.,
RA Allan B., Szymanski C.M.;
RT "Biosynthesis of the N-linked glycan in Campylobacter jejuni and addition
RT onto protein through block transfer.";
RL J. Bacteriol. 188:2427-2434(2006).
CC -!- FUNCTION: Glucosyltransferase that adds he final branching glucose to
CC complete the final heptasaccharide structure in the N-linked protein
CC glycosylation pathway. {ECO:0000269|PubMed:16186480,
CC ECO:0000269|PubMed:16547029}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[alpha-D-GalNAc-(1->4)]4-alpha-D-GalNAc-(1->3)-alpha-D-
CC diNAcBac-tri-trans,hepta-cis-undecaprenyl diphosphate + UDP-alpha-D-
CC glucose = [alpha-D-GalNAc-(1->4)]2-[beta-D-Glc-(1->3)]-[alpha-D-
CC GalNAc-(1->4)]2-alpha-D-GalNAc-(1->3)-alpha-D-diNAcBac-tri-
CC trans,hepta-cis-undecaprenyl diphosphate + H(+) + UDP;
CC Xref=Rhea:RHEA:34523, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:58885, ChEBI:CHEBI:68653, ChEBI:CHEBI:68654;
CC EC=2.4.1.293; Evidence={ECO:0000269|PubMed:16186480};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:16186480}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Loss of the glucose branch in N-glycans. N-
CC glycans however contain the entire 6-mer, demonstrating that Glc plays
CC no role in determining the length of the GalNAc backbone. Cells show
CC levels of colonization of chick cells similar to those of the wild
CC type. {ECO:0000269|PubMed:16547029}.
CC -!- MISCELLANEOUS: N-linked protein glycosylation in C.jejuni consists in
CC the transfer of a heptasaccharide (GalNAc-alpha1,4-GalNAc-alpha1,4-
CC (Glcbeta1,3)-GalNAc-alpha1,4-GalNAc-alpha1,4-GalNAc-alpha1,3-
CC bacillosamine) from a membrane-anchored undecaprenylpyrophosphate (Und-
CC PP)-linked donor to the Asn side chain of proteins at the Asn-X-Ser/Thr
CC motif. {ECO:0000305|PubMed:16186480}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR EMBL; AL111168; CAL35245.1; -; Genomic_DNA.
DR PIR; C81317; C81317.
DR RefSeq; WP_002852770.1; NC_002163.1.
DR RefSeq; YP_002344521.1; NC_002163.1.
DR AlphaFoldDB; Q0P9C6; -.
DR SMR; Q0P9C6; -.
DR IntAct; Q0P9C6; 2.
DR STRING; 192222.Cj1128c; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR PaxDb; Q0P9C6; -.
DR PRIDE; Q0P9C6; -.
DR EnsemblBacteria; CAL35245; CAL35245; Cj1128c.
DR GeneID; 905419; -.
DR KEGG; cje:Cj1128c; -.
DR PATRIC; fig|192222.6.peg.1110; -.
DR eggNOG; COG1215; Bacteria.
DR HOGENOM; CLU_025996_14_0_7; -.
DR OMA; HHADRTF; -.
DR BioCyc; MetaCyc:MON-17334; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046527; F:glucosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Glycosyltransferase; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..309
FT /note="GalNAc(5)-diNAcBac-PP-undecaprenol beta-1,3-
FT glucosyltransferase"
FT /id="PRO_0000422593"
FT TRANSMEM 273..291
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 309 AA; 35511 MW; 9E8E7124DB94A4E8 CRC64;
MPKLSVIVPT FNRQVLLEKA IKSIQNQDFK DLEIIVSDDN SSDDTKSVVQ NLQKDDDRIK
YFLNQNYKQG PNGNKNNGLD QASGEFVTFL DDDDELLSGA LSTLMQKANE GYAHVFGNCL
IEKEGNLSKE FSGKGLEKDS EISKKDFLMA KFSGEFFSVF KKSLLENKRF NEEFYGNEAT
LWVNLYKEKS FYIHKAFRIY RIFRQDSVTL GASKNAYRVY LGYLELAKIL ENELRMSKDK
DYKKTCASYY KMAAYYAKLA KNYKALYKCL FKSLSIKINA PALILLILSI IPNNMIEKLS
KIRVALCKN
