ID   AGLJ_HALVD              Reviewed;         303 AA.
AC   D4GYG3; B5U882;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Glycosyltransferase AglJ;
DE            EC=2.4.1.-;
DE   AltName: Full=Archaeal glycosylation protein J;
GN   Name=aglJ; OrderedLocusNames=HVO_1517;
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,
RP   DISRUPTION PHENOTYPE, AND GENE NAME.
RC   STRAIN=DS2 / DS70;
RX   PubMed=20802039; DOI=10.1128/jb.00705-10;
RA   Kaminski L., Abu-Qarn M., Guan Z., Naparstek S., Ventura V.V., Raetz C.R.,
RA   Hitchen P.G., Dell A., Eichler J.;
RT   "AglJ adds the first sugar of the N-linked pentasaccharide decorating the
RT   Haloferax volcanii S-layer glycoprotein.";
RL   J. Bacteriol. 192:5572-5579(2010).
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 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. Adds the first
CC       hexose subunit of the pentasaccharide to the dolichol phosphate
CC       carrier. {ECO:0000269|PubMed:20802039, ECO:0000269|PubMed:22730124}.
CC   -!- PATHWAY: Cell surface structure biogenesis; S-layer biogenesis.
CC       {ECO:0000269|PubMed:20802039}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Deletion of the gene affects the composition of
CC       the glycan N linked to the S-layer glycoprotein. Also affects the level
CC       of monosaccharide-modified dolichol phosphate. Mutants exhibit
CC       defective or limited motility. {ECO:0000269|PubMed:20802039,
CC       ECO:0000269|PubMed:22730124}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR   EMBL; FM210664; CAR66203.1; -; Genomic_DNA.
DR   EMBL; CP001956; ADE03596.1; -; Genomic_DNA.
DR   RefSeq; WP_013035422.1; NC_013967.1.
DR   AlphaFoldDB; D4GYG3; -.
DR   SMR; D4GYG3; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   EnsemblBacteria; ADE03596; ADE03596; HVO_1517.
DR   GeneID; 8925594; -.
DR   KEGG; hvo:HVO_1517; -.
DR   HOGENOM; CLU_033536_7_3_2; -.
DR   OMA; VCILIPT; -.
DR   BioCyc; MetaCyc:MON-19283; -.
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; IPR026456; GCTrfase_AglJ.
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.
DR   TIGRFAMs; TIGR04182; glyco_TIGR04182; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Glycosyltransferase; Membrane; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..303
FT                   /note="Glycosyltransferase AglJ"
FT                   /id="PRO_0000415355"
FT   TRANSMEM        230..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        263..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   303 AA;  33270 MW;  CEB6849FE468B55C CRC64;
     MPTPDAVCIL TPTYNEAETI ADVISDYRDE GFANVLVIDG GSTDGTRELA EDAGAHVVVQ
     SGSGKGQAVR EAVEDHIQAP YVLMLDGDGT YEATDATKML DPLTEGYDHV IGDRFADMRP
     GAMTRLNRVG NRIINRAFAF IHGQDFRDIL SGYRAFTRES FLDMTLTSDG FGIETEMAVE
     CAKRGIKTTV VPTTYYPRPD GSDTNLDPIR DGGIIFLELY RRAKTNNPLF YFGSVGFAST
     ATGLGLALYV AYEWVVRSIS HEVIAVVSMA GILFGVQLLM FGVLSDLILS LHREQMKRIE
     ELE