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GalNAc-alpha-(1->4)-GalNAc-alpha-(1->3)-diNAcBac-PP-undecaprenol alpha-1,4-N-acetyl-D-galactosaminyltransferase (EC 2.4.1.292) (Protein glycosylation H)

 PGLH_CAMJE              Reviewed;         359 AA.
Q0P9C5;
29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
19-SEP-2006, sequence version 1.
23-MAY-2018, entry version 61.
RecName: Full=GalNAc-alpha-(1->4)-GalNAc-alpha-(1->3)-diNAcBac-PP-undecaprenol alpha-1,4-N-acetyl-D-galactosaminyltransferase;
EC=2.4.1.292;
AltName: Full=Protein glycosylation H;
Name=pglH; OrderedLocusNames=Cj1129c;
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 /
NCTC 11168).
Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
Campylobacteraceae; Campylobacter.
NCBI_TaxID=192222;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700819 / NCTC 11168;
PubMed=10688204; DOI=10.1038/35001088;
Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W.,
Quail M.A., Rajandream M.A., Rutherford K.M., van Vliet A.H.M.,
Whitehead S., Barrell B.G.;
"The genome sequence of the food-borne pathogen Campylobacter jejuni
reveals hypervariable sequences.";
Nature 403:665-668(2000).
[2]
FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
STRAIN=ATCC 700819 / NCTC 11168;
PubMed=16186480; DOI=10.1073/pnas.0507311102;
Glover K.J., Weerapana E., Imperiali B.;
"In vitro assembly of the undecaprenylpyrophosphate-linked
heptasaccharide for prokaryotic N-linked glycosylation.";
Proc. Natl. Acad. Sci. U.S.A. 102:14255-14259(2005).
[3]
FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLU-42; GLU-50;
GLU-172; GLU-180; ARG-190; GLU-266; GLU-274; GLU-309; GLU-317; GLU-347
AND GLU-355.
PubMed=19159314; DOI=10.1021/bi802284d;
Troutman J.M., Imperiali B.;
"Campylobacter jejuni PglH is a single active site processive
polymerase that utilizes product inhibition to limit sequential
glycosyl transfer reactions.";
Biochemistry 48:2807-2816(2009).
-!- FUNCTION: Transfers 3 terminal GalNAc residues to the carrier
polyisoprene in the N-linked protein glycosylation pathway. Acts
as a polymerase via a processive reaction in which intermediates
do not dissociate from the enzyme and by using a single active
site for multiple GalNAc transfers. Uses product inhibition to
stop the enzyme from carrying out more than 3 GalNAc transfer
reactions. {ECO:0000269|PubMed:16186480,
ECO:0000269|PubMed:19159314}.
-!- CATALYTIC ACTIVITY: 3 UDP-N-acetyl-alpha-D-galactosamine + GalNAc-
alpha-(1->4)-GalNAc-alpha-(1->3)-diNAcBac-PP-tritrans,heptacis-
undecaprenol = 3 UDP + (GalNAc-alpha-(1->4))(4)-GalNAc-alpha-
(1->3)-diNAcBac-PP-tritrans,heptacis-undecaprenol.
{ECO:0000269|PubMed:16186480, ECO:0000269|PubMed:19159314}.
-!- PATHWAY: Protein modification; protein glycosylation.
{ECO:0000269|PubMed:16186480}.
-!- MISCELLANEOUS: N-linked protein glycosylation in C.jejuni consists
in the transfer of a heptasaccharide (GalNAc-alpha1,4-GalNAc-
alpha1,4-(Glcbeta1,3)-GalNAc-alpha1,4-GalNAc-alpha1,4-GalNAc-
alpha1,3-bacillosamine) from a membrane-anchored
undecaprenylpyrophosphate (Und-PP)-linked donor to the Asn side
chain of proteins at the Asn-X-Ser/Thr motif.
{ECO:0000305|PubMed:16186480}.
-!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
{ECO:0000305}.
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EMBL; AL111168; CAL35246.1; -; Genomic_DNA.
PIR; D81317; D81317.
RefSeq; YP_002344522.1; NC_002163.1.
ProteinModelPortal; Q0P9C5; -.
SMR; Q0P9C5; -.
IntAct; Q0P9C5; 1.
STRING; 192222.Cj1129c; -.
CAZy; GT4; Glycosyltransferase Family 4.
PaxDb; Q0P9C5; -.
PRIDE; Q0P9C5; -.
EnsemblBacteria; CAL35246; CAL35246; Cj1129c.
GeneID; 905420; -.
KEGG; cje:Cj1129c; -.
PATRIC; fig|192222.6.peg.1111; -.
eggNOG; ENOG4105CG5; Bacteria.
eggNOG; COG0438; LUCA.
HOGENOM; HOG000077289; -.
KO; K17249; -.
OMA; SSRYEGW; -.
BioCyc; CJEJ192222:G1G1F-1088-MONOMER; -.
BioCyc; MetaCyc:MONOMER-17333; -.
UniPathway; UPA00378; -.
Proteomes; UP000000799; Chromosome.
GO; GO:0016758; F:transferase activity, transferring hexosyl groups; IDA:UniProtKB.
GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IDA:UniProtKB.
InterPro; IPR001296; Glyco_trans_1.
InterPro; IPR028098; Glyco_trans_4-like_N.
Pfam; PF13439; Glyco_transf_4; 1.
Pfam; PF00534; Glycos_transf_1; 1.
1: Evidence at protein level;
Complete proteome; Glycosyltransferase; Reference proteome;
Transferase.
CHAIN 1 359 GalNAc-alpha-(1->4)-GalNAc-alpha-(1->3)-
diNAcBac-PP-undecaprenol alpha-1,4-N-
acetyl-D-galactosaminyltransferase.
/FTId=PRO_0000422591.
MUTAGEN 42 42 E->A: No effect.
{ECO:0000269|PubMed:19159314}.
MUTAGEN 50 50 E->A: No effect.
{ECO:0000269|PubMed:19159314}.
MUTAGEN 172 172 E->A: No effect.
{ECO:0000269|PubMed:19159314}.
MUTAGEN 180 180 E->A: No effect.
{ECO:0000269|PubMed:19159314}.
MUTAGEN 190 190 R->A: Abolishes catalytic activity.
{ECO:0000269|PubMed:19159314}.
MUTAGEN 266 266 E->A: Abolishes catalytic activity.
{ECO:0000269|PubMed:19159314}.
MUTAGEN 274 274 E->A: Abolishes catalytic activity.
{ECO:0000269|PubMed:19159314}.
MUTAGEN 309 309 E->A: No effect.
{ECO:0000269|PubMed:19159314}.
MUTAGEN 317 317 E->A: No effect.
{ECO:0000269|PubMed:19159314}.
MUTAGEN 347 347 E->A: No effect.
{ECO:0000269|PubMed:19159314}.
MUTAGEN 355 355 E->A: No effect.
{ECO:0000269|PubMed:19159314}.
SEQUENCE 359 AA; 41163 MW; 34BCDBFC41A1FF77 CRC64;
MMKISFIIAT LNSGGAERAL VTLANALCKE HEVSIIKFHA GESFYKLENE VKVTSLEQFR
FDTLYHKIAS RFKKFFALRK ALKESKSDVF ISFLDTTNIA CIAAKIGLKT PLIISEHSNE
AYLKPKIWRF LRRVSYPFCD ALSVLGSSDK VYYERFVKRV KLLLNPCHFS DEISFDSSFE
KENLVLFIGR LDHNKNPVMF LKAIAHLDKN LQENYKFVIA GDGQLRQELE YKVKSLGIKV
DFLGRVENVK ALYEKAKVLC LCSFVEGLPT VLIESLYFEV CRISSSYYNG AKDLIKDNHD
GLLVGCDDEI ALAKKLELVL NDENFRKELV NNAKQRCKDF EISHIKEEWL KLIAEVKNA


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