ID   PGLC_CAMJE              Reviewed;         200 AA.
AC   Q0P9D0;
DT   29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Undecaprenyl phosphate N,N'-diacetylbacillosamine 1-phosphate transferase;
DE            EC=2.7.8.36;
DE   AltName: Full=Protein glycosylation C;
GN   Name=pglC; OrderedLocusNames=Cj1124c;
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, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=16618123; DOI=10.1021/bi0602056;
RA   Glover K.J., Weerapana E., Chen M.M., Imperiali B.;
RT   "Direct biochemical evidence for the utilization of UDP-bacillosamine by
RT   PglC, an essential glycosyl-1-phosphate transferase in the Campylobacter
RT   jejuni N-linked glycosylation pathway.";
RL   Biochemistry 45:5343-5350(2006).
CC   -!- FUNCTION: Glycosyl-1-phosphate transferase that mediates the first step
CC       in the biosynthesis of the undecaprenyl-linked heptasaccharide donor in
CC       the N-linked protein glycosylation pathway. Catalyzes the linking of
CC       uridine 5'-diphosphobacillosamine (UDP-Bac) to undecaprenyl phosphate
CC       to create the first membrane-associated intermediate
CC       undecaprenylpyrophosphate-linked Bac (Und-PP-Bac).
CC       {ECO:0000269|PubMed:16618123}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=tri-trans,hepta-cis-undecaprenyl phosphate + UDP-N,N'-
CC         diacetylbacillosamine = N,N'-diacetyl-alpha-D-bacillosaminyl-tri-
CC         trans,hepta-cis-undecaprenyl diphosphate + UMP; Xref=Rhea:RHEA:34515,
CC         ChEBI:CHEBI:57865, ChEBI:CHEBI:67134, ChEBI:CHEBI:68672,
CC         ChEBI:CHEBI:70763; EC=2.7.8.36;
CC         Evidence={ECO:0000269|PubMed:16618123};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=6.2 uM for uridine 5'-diphosphobacillosamine
CC         {ECO:0000269|PubMed:16618123};
CC         KM=4.3 uM for UDP-6-hydroxybacillosamine
CC         {ECO:0000269|PubMed:16618123};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000269|PubMed:16618123}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:16618123}; Single-
CC       pass membrane protein {ECO:0000305|PubMed:16618123}.
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.
CC   -!- SIMILARITY: Belongs to the bacterial sugar transferase family.
CC       {ECO:0000305}.
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DR   EMBL; AL111168; CAL35241.1; -; Genomic_DNA.
DR   PIR; G81316; G81316.
DR   RefSeq; WP_002852766.1; NC_002163.1.
DR   RefSeq; YP_002344517.1; NC_002163.1.
DR   AlphaFoldDB; Q0P9D0; -.
DR   SMR; Q0P9D0; -.
DR   IntAct; Q0P9D0; 1.
DR   STRING; 192222.Cj1124c; -.
DR   PaxDb; Q0P9D0; -.
DR   PRIDE; Q0P9D0; -.
DR   EnsemblBacteria; CAL35241; CAL35241; Cj1124c.
DR   GeneID; 905415; -.
DR   KEGG; cje:Cj1124c; -.
DR   PATRIC; fig|192222.6.peg.1106; -.
DR   eggNOG; COG2148; Bacteria.
DR   HOGENOM; CLU_024920_1_4_7; -.
DR   OMA; QVQNIDM; -.
DR   BioCyc; MetaCyc:MON-17321; -.
DR   BRENDA; 2.7.8.36; 13746.
DR   SABIO-RK; Q0P9D0; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000000799; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0102334; F:N,N'-diacetylbacilliosaminyl-1-phosphate transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IDA:UniProtKB.
DR   GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IDA:UniProtKB.
DR   InterPro; IPR003362; Bact_transf.
DR   Pfam; PF02397; Bac_transf; 1.
PE   1: Evidence at protein level;
KW   Glycosyltransferase; Membrane; Reference proteome; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..200
FT                   /note="Undecaprenyl phosphate N,N'-diacetylbacillosamine 1-
FT                   phosphate transferase"
FT                   /id="PRO_0000422586"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   200 AA;  23144 MW;  9A0BF5A28A497B0C CRC64;
     MYEKVFKRIF DFILALVLLV LFSPVILITA LLLKITQGSV IFTQNRPGLD EKIFKIYKFK
     TMSDERDEKG ELLSDELRLK AFGKIVRSLS LDELLQLFNV LKGDMSFVGP RPLLVEYLPL
     YNKEQKLRHK VRPGITGWAQ VNGRNAISWQ KKFELDVYYV KNISFLLDLK IMFLTALKVL
     KRSGVSKEGH VTTEKFNGKN