ID   PGLA_CAMJE              Reviewed;         376 AA.
AC   Q0P9C9;
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=N,N'-diacetylbacillosaminyl-diphospho-undecaprenol alpha-1,3-N-acetylgalactosaminyltransferase;
DE            EC=2.4.1.290;
DE   AltName: Full=Protein glycosylation A;
GN   Name=pglA; OrderedLocusNames=Cj1125c;
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).
CC   -!- FUNCTION: Adds the first GalNAc residue on to the isoprenoid-linked
CC       bacillosamine (2,4-diacetamido-2,4,6-trideoxyglucose) carrier in the N-
CC       linked protein glycosylation pathway. Acts first on the
CC       undecaprenylpyrophosphate-linked bacillosamine (Und-PP-Bac) substrate
CC       to yield the disaccharide. {ECO:0000269|PubMed:16186480}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N,N'-diacetyl-alpha-D-bacillosaminyl-tri-trans,hepta-cis-
CC         undecaprenyl diphosphate + UDP-N-acetyl-alpha-D-galactosamine = H(+)
CC         + N-acetyl-alpha-D-galactosaminyl-(1->3)-N,N'-diacetyl-alpha-D-
CC         bacillosaminyl-tri-trans,hepta-cis-undecaprenyl diphosphate + UDP;
CC         Xref=Rhea:RHEA:34511, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:67138, ChEBI:CHEBI:68652, ChEBI:CHEBI:68672;
CC         EC=2.4.1.290; Evidence={ECO:0000269|PubMed:16186480};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000269|PubMed:16186480}.
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; CAL35242.1; -; Genomic_DNA.
DR   PIR; H81316; H81316.
DR   RefSeq; WP_002852885.1; NC_002163.1.
DR   RefSeq; YP_002344518.1; NC_002163.1.
DR   AlphaFoldDB; Q0P9C9; -.
DR   SMR; Q0P9C9; -.
DR   IntAct; Q0P9C9; 4.
DR   STRING; 192222.Cj1125c; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   PaxDb; Q0P9C9; -.
DR   PRIDE; Q0P9C9; -.
DR   EnsemblBacteria; CAL35242; CAL35242; Cj1125c.
DR   GeneID; 905416; -.
DR   KEGG; cje:Cj1125c; -.
DR   PATRIC; fig|192222.6.peg.1107; -.
DR   eggNOG; COG0438; Bacteria.
DR   HOGENOM; CLU_009583_8_1_7; -.
DR   OMA; SYYREGI; -.
DR   BioCyc; MetaCyc:MON-17322; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000000799; Chromosome.
DR   GO; GO:0016758; F:hexosyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0102335; F:N,N'-diacetylbacillosaminyl-diphospho-undecaprenol alpha-1,3-N-acetylgalactosaminyltransferase activity; IEA:UniProtKB-EC.
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; PF13477; Glyco_trans_4_2; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
PE   1: Evidence at protein level;
KW   Glycosyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..376
FT                   /note="N,N'-diacetylbacillosaminyl-diphospho-undecaprenol
FT                   alpha-1,3-N-acetylgalactosaminyltransferase"
FT                   /id="PRO_0000422590"
SQ   SEQUENCE   376 AA;  42816 MW;  E385AB54635972E8 CRC64;
     MRIGFLSHAG ASIYHFRMPI IKALKDRKDE VFVIVPQDEY TQKLRDLGLK VIVYEFSRAS
     LNPFVVLKNF FYLAKVLKNL NLDFIQSAAH KSNTFGILAA KWAKIPYRFA LVEGLGSFYI
     DQGFKANLVR FVINSLYKLS FKFAHQFIFV NESNAEFMRN LGLKENKICV IKSVGINLKK
     FFPIYVESEK KELFWKNLNI DKKPIVLMIA RALWHKGVKE FYESATMLKD KANFVLVGGR
     DENPSCASLE FLNSGAVHYL GARSDIVELL QNCDIFVLPS YKEGFPVSVL EAKACGKAIV
     VSDCEGCVEA ISNAYDGLWA KTKNAKDLSE KISLLLEDEK LRLNLAKNAA QDALQYDENI
     IAQRYLKLYD RVIKNV