ID   AGLI_HALVD              Reviewed;         295 AA.
AC   D4GYH2; B2G4W6;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=Glycosyltransferase AglI;
DE            EC=2.4.1.-;
DE   AltName: Full=Archaeal glycosylation protein I;
GN   Name=aglI; OrderedLocusNames=HVO_1528;
OS   Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS   NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=309800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN GLYCOSYLATION, PATHWAY, AND
RP   GENE NAME.
RC   STRAIN=DS2 / DS70;
RX   PubMed=18631242; DOI=10.1111/j.1365-2958.2008.06352.x;
RA   Yurist-Doutsch S., Abu-Qarn M., Battaglia F., Morris H.R., Hitchen P.G.,
RA   Dell A., Eichler J.;
RT   "AglF, aglG and aglI, novel members of a gene island involved in the N-
RT   glycosylation of the Haloferax volcanii S-layer glycoprotein.";
RL   Mol. Microbiol. 69:1234-1245(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC   B-1768 / DS2;
RX   PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA   Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA   Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA   Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT   "The complete genome sequence of Haloferax volcanii DS2, a model
RT   archaeon.";
RL   PLoS ONE 5:E9605-E9605(2010).
RN   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=H53;
RX   PubMed=21091511; DOI=10.1111/j.1365-2958.2010.07405.x;
RA   Guan Z., Naparstek S., Kaminski L., Konrad Z., Eichler J.;
RT   "Distinct glycan-charged phosphodolichol carriers are required for the
RT   assembly of the pentasaccharide N-linked to the Haloferax volcanii S-layer
RT   glycoprotein.";
RL   Mol. Microbiol. 78:1294-1303(2010).
RN   [4]
RP   FUNCTION IN GLYCOSYLATION OF FLAGELLINS, AND DISRUPTION PHENOTYPE.
RC   STRAIN=H53;
RX   PubMed=22730124; DOI=10.1128/jb.00731-12;
RA   Tripepi M., You J., Temel S., Onder O., Brisson D., Pohlschroder M.;
RT   "N-glycosylation of Haloferax volcanii flagellins requires known Agl
RT   proteins and is essential for biosynthesis of stable flagella.";
RL   J. Bacteriol. 194:4876-4887(2012).
CC   -!- FUNCTION: Involved in the assembly of a N-linked pentasaccharide that
CC       decorates the S-layer glycoprotein and flagellins. Catalyzes the
CC       addition to the dolichol phosphate carrier of the hexuronic acid found
CC       at position 3 of the pentasaccharide. {ECO:0000269|PubMed:18631242,
CC       ECO:0000269|PubMed:21091511, ECO:0000269|PubMed:22730124}.
CC   -!- PATHWAY: Cell surface structure biogenesis; S-layer biogenesis.
CC       {ECO:0000269|PubMed:18631242}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Mutants contain only mono- and disaccharide-
CC       modified phosphodolichols and exhibit defective or limited motility.
CC       {ECO:0000269|PubMed:21091511, ECO:0000269|PubMed:22730124}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR   EMBL; AM991129; CAQ51230.1; -; Genomic_DNA.
DR   EMBL; CP001956; ADE04584.1; -; Genomic_DNA.
DR   RefSeq; WP_013035575.1; NC_013967.1.
DR   AlphaFoldDB; D4GYH2; -.
DR   SMR; D4GYH2; -.
DR   STRING; 309800.C498_02995; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   EnsemblBacteria; ADE04584; ADE04584; HVO_1528.
DR   GeneID; 8925953; -.
DR   KEGG; hvo:HVO_1528; -.
DR   eggNOG; arCOG01385; Archaea.
DR   HOGENOM; CLU_025996_19_6_2; -.
DR   OMA; FQPRSFN; -.
DR   OrthoDB; 65802at2157; -.
DR   BioCyc; MetaCyc:MON-19285; -.
DR   UniPathway; UPA00977; -.
DR   Proteomes; UP000008243; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0045232; P:S-layer organization; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR001173; Glyco_trans_2-like.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   Pfam; PF00535; Glycos_transf_2; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Glycosyltransferase; Membrane; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..295
FT                   /note="Glycosyltransferase AglI"
FT                   /id="PRO_0000415419"
FT   TRANSMEM        265..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   295 AA;  32846 MW;  8D513D8710954F13 CRC64;
     MADSPFPCVS VIVPVYNDPT GIRDTLTALT KQTYPTERVN ILPIDNGSTD ETRDVIRQFE
     REHENVTLVV EDEIQGSYAA RNTGIEQATG EIFAFVDADM YMDESWLETA VDAMDEAAYV
     GCDIELVTNG EDTLPARFDA QTAFPIAQYI RQQQYAPTCG LLVSREVVDD VGPFDERLVS
     GGDSEFGSRV ANAGYRQAFA PAATLYHPVR DSFSSLVKKE LRVGRGLCQR QEYYADRFGR
     PGIPPRPSGV KSPDEESSGL DFERLLFGVL SVVMTGVRAL GYYREYVRYV RGNTR