ID   AGL16_SULAC             Reviewed;         352 AA.
AC   Q4JAK2;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Archaeal glycosylation protein 16;
DE            EC=2.4.1.-;
GN   Name=agl16; OrderedLocusNames=Saci_0807;
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS   15157 / NCIMB 11770).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
RN   [2]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX   PubMed=23475978; DOI=10.1128/jb.00035-13;
RA   Meyer B.H., Peyfoon E., Dietrich C., Hitchen P., Panico M., Morris H.R.,
RA   Dell A., Albers S.V.;
RT   "Agl16, a thermophilic glycosyltransferase mediating the last step of N-
RT   Glycan biosynthesis in the thermoacidophilic crenarchaeon Sulfolobus
RT   acidocaldarius.";
RL   J. Bacteriol. 195:2177-2186(2013).
CC   -!- FUNCTION: Glycosyltransferase catalyzing the last biosynthesis step of
CC       the N-glycan biosynthesis. {ECO:0000269|PubMed:23475978}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000269|PubMed:23475978}.
CC   -!- PATHWAY: Cell surface structure biogenesis; S-layer biogenesis.
CC       {ECO:0000269|PubMed:23475978}.
CC   -!- DISRUPTION PHENOTYPE: Reduced molecular weights of the S-layer
CC       glycoprotein and archaellins due to a change in the N-glycan
CC       composition. The tribranched hexasaccharide glycan of S-layer
CC       glycoprotein is a pentasaccharide that lacks a terminal hexose residue.
CC       {ECO:0000269|PubMed:23475978}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC       Glycosyltransferase 4 subfamily. {ECO:0000305}.
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DR   EMBL; CP000077; AAY80177.1; -; Genomic_DNA.
DR   RefSeq; WP_011277679.1; NC_007181.1.
DR   AlphaFoldDB; Q4JAK2; -.
DR   SMR; Q4JAK2; -.
DR   STRING; 330779.Saci_0807; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   EnsemblBacteria; AAY80177; AAY80177; Saci_0807.
DR   GeneID; 3472645; -.
DR   KEGG; sai:Saci_0807; -.
DR   PATRIC; fig|330779.12.peg.773; -.
DR   eggNOG; arCOG01403; Archaea.
DR   HOGENOM; CLU_009583_2_2_2; -.
DR   OMA; HTTRDTY; -.
DR   UniPathway; UPA00378; -.
DR   UniPathway; UPA00977; -.
DR   Proteomes; UP000001018; Chromosome.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   GO; GO:0045232; P:S-layer organization; IEA:UniProtKB-UniPathway.
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   3: Inferred from homology;
KW   Glycosyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..352
FT                   /note="Archaeal glycosylation protein 16"
FT                   /id="PRO_0000428778"
SQ   SEQUENCE   352 AA;  40625 MW;  30A1D659BF3B8471 CRC64;
     MYKVWMLTPL FLPVRGGTEV HVFNLSRELV KMSIDVEVHT TRDTYTEREK LIPFEIMDGI
     KVVRHKRTWI YRDSPSVLHF HNLGRKFSTW NLYTFLFFSL PSVEAPLVMT PHHIFVSDQG
     RVINWLKRNI GKRVDKLIAV SEWEKEEMIN LGYDGSKIVV IPNGVDDMAF NYPKSEGFED
     YLLYIGRISP EKNQLFAIEC IKNLNVKLIL IGQVRDKDYL EKIMTRVSEL GLEDKVRYLG
     VVTEEEKYSL MDKSLAVILT SDIEAEGIVI KEAMVRGVPV IVGNKAKVLS TIVKDGVNGF
     VISSCQDLKD AVEKLRDPKV RKEIGENNIS ISREWRWRNV SLKVLELYKS LS