PGLJ_CAMJE
ID PGLJ_CAMJE Reviewed; 365 AA.
AC Q0P9C7;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=N-acetylgalactosamine-N,N'-diacetylbacillosaminyl-diphospho-undecaprenol 4-alpha-N-acetylgalactosaminyltransferase;
DE EC=2.4.1.291;
DE AltName: Full=Protein glycosylation J;
GN Name=pglJ; OrderedLocusNames=Cj1127c;
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 SUBCELLULAR LOCATION.
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=18034500; DOI=10.1021/bi701956x;
RA Chen M.M., Weerapana E., Ciepichal E., Stupak J., Reid C.W., Swiezewska E.,
RA Imperiali B.;
RT "Polyisoprenol specificity in the Campylobacter jejuni N-linked
RT glycosylation pathway.";
RL Biochemistry 46:14342-14348(2007).
CC -!- FUNCTION: Adds a GalNAc residue on to the Und-PP-Bac2,4diNAc-GalNAc
CC disaccharide in the N-linked protein glycosylation pathway. Transfers
CC the third sugar in the heptasaccharide biosynthesis.
CC {ECO:0000269|PubMed:16186480, ECO:0000269|PubMed:18034500}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-acetyl-alpha-D-galactosaminyl-(1->3)-N,N'-diacetyl-alpha-D-
CC bacillosaminyl-tri-trans,hepta-cis-undecaprenyl diphosphate + UDP-N-
CC acetyl-alpha-D-galactosamine = H(+) + N-acetyl-alpha-D-
CC galactosaminyl-(1->4)-N-acetyl-alpha-D-galactosaminyl-(1->3)-N,N'-
CC diacetyl-alpha-D-bacillosaminyl-tri-trans,heptacis-undecaprenyl
CC diphosphate + UDP; Xref=Rhea:RHEA:34543, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:67138, ChEBI:CHEBI:68651,
CC ChEBI:CHEBI:68652; EC=2.4.1.291;
CC Evidence={ECO:0000269|PubMed:16186480};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:16186480}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:18034500}; Peripheral membrane protein
CC {ECO:0000305|PubMed:18034500}.
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 group 1 family.
CC {ECO:0000305}.
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DR EMBL; AL111168; CAL35244.1; -; Genomic_DNA.
DR PIR; B81317; B81317.
DR RefSeq; WP_002852870.1; NC_002163.1.
DR RefSeq; YP_002344520.1; NC_002163.1.
DR AlphaFoldDB; Q0P9C7; -.
DR SMR; Q0P9C7; -.
DR STRING; 192222.Cj1127c; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR PaxDb; Q0P9C7; -.
DR PRIDE; Q0P9C7; -.
DR DNASU; 905418; -.
DR EnsemblBacteria; CAL35244; CAL35244; Cj1127c.
DR GeneID; 905418; -.
DR KEGG; cje:Cj1127c; -.
DR PATRIC; fig|192222.6.peg.1109; -.
DR eggNOG; COG0438; Bacteria.
DR HOGENOM; CLU_009583_0_0_7; -.
DR OMA; NGILCEL; -.
DR BioCyc; MetaCyc:MON-17332; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016758; F:hexosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IDA:UniProtKB.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR028098; Glyco_trans_4-like_N.
DR Pfam; PF13439; Glyco_transf_4; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Glycosyltransferase; Membrane;
KW Reference proteome; Transferase.
FT CHAIN 1..365
FT /note="N-acetylgalactosamine-N,N'-diacetylbacillosaminyl-
FT diphospho-undecaprenol 4-alpha-N-
FT acetylgalactosaminyltransferase"
FT /id="PRO_0000422592"
SQ SEQUENCE 365 AA; 41308 MW; 4056FD1664FE8A40 CRC64;
MQKLGIFIYS LGSGGAERVV ATLLPILSLK FEVHLILMND KISYEIPECQ IHFLECSKPS
ENPILKFLKL PFLALKYKKL CRNLGIDTEF VFLNRPNYIA LMARMFGNKT RLVINECTTP
SVMYMKNNFN SLVNKFLISL LYPKADLILP NSKGNLEDLV QNFSISPKKC EILYNAIDLE
NIGQKALEDI ALKDKFILSV GRLDKGKNHA LLIRAYARLK TDLKLVILGE GVLKDELLAL
IKELNLEEKV LLLGFDNNPY KYMAKCEFFA FASVFEGFSN VLIESLACSC AVVCTDHKSG
ARELFGDDEF GLLVEVDNEN SMFQGLKTML EDDKLRKAYK NKAKTRAKAF DKVKIARDAL
KYLLG
