ID   AGLE_HALVD              Reviewed;         304 AA.
AC   D4GYG7; A8E1V5;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Glycosyltransferase AglE;
DE            EC=2.4.1.-;
DE   AltName: Full=Archaeal glycosylation protein E;
GN   Name=aglE; OrderedLocusNames=HVO_1523.1; ORFNames=HVO_1523A;
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   SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND GENE NAME.
RC   STRAIN=DS2 / DS70;
RX   PubMed=18310347; DOI=10.1128/jb.00056-08;
RA   Abu-Qarn M., Giordano A., Battaglia F., Trauner A., Hitchen P.G.,
RA   Morris H.R., Dell A., Eichler J.;
RT   "Identification of AglE, a second glycosyltransferase involved in N
RT   glycosylation of the Haloferax volcanii S-layer glycoprotein.";
RL   J. Bacteriol. 190:3140-3146(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 4 of the pentasaccharide. {ECO:0000269|PubMed:18310347,
CC       ECO:0000269|PubMed:21091511, ECO:0000269|PubMed:22730124}.
CC   -!- PATHWAY: Cell surface structure biogenesis; S-layer biogenesis.
CC       {ECO:0000269|PubMed:18310347}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18310347}.
CC       Note=Could be an integral membrane protein.
CC   -!- DISRUPTION PHENOTYPE: Mutants contain only mono-, di- and
CC       trisaccharide-modified phosphodolichols. Deletion does not alter cell
CC       growth or stability of the S-layer. Mutants exhibit defective or
CC       limited motility. {ECO:0000269|PubMed:18310347,
CC       ECO:0000269|PubMed:21091511, ECO:0000269|PubMed:22730124}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AM888352; CAP09656.1; -; Genomic_DNA.
DR   EMBL; CP001956; ADE02271.1; -; Genomic_DNA.
DR   AlphaFoldDB; D4GYG7; -.
DR   SMR; D4GYG7; -.
DR   STRING; 309800.C498_02970; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   EnsemblBacteria; ADE02271; ADE02271; HVO_1523A.
DR   KEGG; hvo:HVO_1523A; -.
DR   eggNOG; arCOG01385; Archaea.
DR   HOGENOM; CLU_025996_19_6_2; -.
DR   OMA; TANVFTF; -.
DR   BioCyc; MetaCyc:MON-19286; -.
DR   UniPathway; UPA00977; -.
DR   Proteomes; UP000008243; Chromosome.
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.
FT   CHAIN           1..304
FT                   /note="Glycosyltransferase AglE"
FT                   /id="PRO_0000415353"
SQ   SEQUENCE   304 AA;  33869 MW;  2BC928799A4916DE CRC64;
     MTSTLPFVSV IIPVYNEAEN IQKCLNAVTS QTYPKSKYEV LVVDNGSQDG TKEIARQFST
     AYDNLEILIE DEQQGSYAAR NTGIEQSSGA ILAFLDGDCS PHQQWLERGV STISGTGVDL
     VGGNVEFTYP NGGTAAERYD SFTNMQMKES ISKRNVAKTV NLFVRQDVVE DVGPFPNHLI
     SGGDVHWTKR ATDAGYSLTF AHDVIGCHPA RPFGELLKKQ FRVGKGQIQV WMLDRISLRR
     VFALALWILV GFLPKPPHYL SQDLRRTGQT VTKAMFVRIL VVAWCCRLAE NAGRLSYILR
     SEEQ