ID   AGLQ_HALVD              Reviewed;         371 AA.
AC   D4GYG6; B7VU78;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Archaeal glycosylation protein Q;
GN   Name=aglQ; OrderedLocusNames=HVO_1523; ORFNames=C498_02965;
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], AND GENE NAME.
RX   PubMed=19251857; DOI=10.1128/jb.01838-08;
RA   Yurist-Doutsch S., Eichler J.;
RT   "Manual annotation, transcriptional analysis, and protein expression
RT   studies reveal novel genes in the agl cluster responsible for N
RT   glycosylation in the halophilic archaeon Haloferax volcanii.";
RL   J. Bacteriol. 191:3068-3075(2009).
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   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=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, PATHWAY, DISRUPTION PHENOTYPE, AND
RP   MUTAGENESIS OF HIS-34; GLU-37; THR-38; PHE-50; LYS-52; GLU-55; ASP-58;
RP   GLU-59; ARG-61; ALA-66; HIS-81; LYS-93; TRP-104; ARG-114; ASN-118 AND
RP   ASP-187.
RX   PubMed=24236216; DOI=10.1371/journal.pone.0081782;
RA   Arbiv A., Yurist-Doutsch S., Guan Z., Eichler J.;
RT   "AglQ is a novel component of the Haloferax volcanii N-glycosylation
RT   pathway.";
RL   PLoS ONE 8:E81782-E81782(2013).
CC   -!- FUNCTION: Putative isomerase involved in the N-glycosylation pathway.
CC       Required for the appearance of the methyl ester of hexuronic acid found
CC       at position four of the pentasaccharide N-linked to the S-layer
CC       glycoprotein. Either involved in preparing the third sugar for
CC       attachment of the fourth pentasaccharide subunit or processing the
CC       fourth sugar prior to its addition to the lipid-linked trisaccharide.
CC       {ECO:0000269|PubMed:24236216}.
CC   -!- PATHWAY: Cell surface structure biogenesis; S-layer biogenesis.
CC       {ECO:0000269|PubMed:24236216}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:24236216}.
CC   -!- DISRUPTION PHENOTYPE: Defects in N-glycosylation pathway, characterized
CC       by impaired addition of the fourth sugar of the pentasaccharide: both
CC       dolichol phosphate, the lipid carrier used in H.volcanii N-
CC       glycosylation, and modified S-layer glycoprotein Asn residues only
CC       present the first three subunits of the pentasaccharide.
CC       {ECO:0000269|PubMed:24236216}.
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DR   EMBL; FM955370; CAW30728.1; -; Genomic_DNA.
DR   EMBL; CP001956; ADE02297.1; -; Genomic_DNA.
DR   EMBL; AOHU01000027; ELY35857.1; -; Genomic_DNA.
DR   AlphaFoldDB; D4GYG6; -.
DR   SMR; D4GYG6; -.
DR   STRING; 309800.C498_02965; -.
DR   EnsemblBacteria; ADE02297; ADE02297; HVO_1523.
DR   EnsemblBacteria; ELY35857; ELY35857; C498_02965.
DR   KEGG; hvo:HVO_1523; -.
DR   PATRIC; fig|309800.29.peg.570; -.
DR   eggNOG; arCOG09256; Archaea.
DR   HOGENOM; CLU_745158_0_0_2; -.
DR   OMA; VRTTSHW; -.
DR   BioCyc; MetaCyc:MON-20385; -.
DR   UniPathway; UPA00977; -.
DR   Proteomes; UP000008243; Chromosome.
DR   Proteomes; UP000011532; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0045232; P:S-layer organization; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   SUPFAM; SSF48208; SSF48208; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Reference proteome.
FT   CHAIN           1..371
FT                   /note="Archaeal glycosylation protein Q"
FT                   /id="PRO_0000428767"
FT   REGION          19..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         34
FT                   /note="H->D: No effect."
FT                   /evidence="ECO:0000269|PubMed:24236216"
FT   MUTAGEN         37
FT                   /note="E->A: No effect."
FT                   /evidence="ECO:0000269|PubMed:24236216"
FT   MUTAGEN         38
FT                   /note="T->L: Defects in N-glycosylation pathway."
FT                   /evidence="ECO:0000269|PubMed:24236216"
FT   MUTAGEN         50
FT                   /note="F->A: No effect."
FT                   /evidence="ECO:0000269|PubMed:24236216"
FT   MUTAGEN         52
FT                   /note="K->L: Defects in N-glycosylation pathway."
FT                   /evidence="ECO:0000269|PubMed:24236216"
FT   MUTAGEN         55
FT                   /note="E->K: No effect."
FT                   /evidence="ECO:0000269|PubMed:24236216"
FT   MUTAGEN         58
FT                   /note="D->A: No effect."
FT                   /evidence="ECO:0000269|PubMed:24236216"
FT   MUTAGEN         59
FT                   /note="E->A: No effect."
FT                   /evidence="ECO:0000269|PubMed:24236216"
FT   MUTAGEN         61
FT                   /note="R->D: No effect."
FT                   /evidence="ECO:0000269|PubMed:24236216"
FT   MUTAGEN         66
FT                   /note="A->Q: No effect."
FT                   /evidence="ECO:0000269|PubMed:24236216"
FT   MUTAGEN         81
FT                   /note="H->D: No effect."
FT                   /evidence="ECO:0000269|PubMed:24236216"
FT   MUTAGEN         93
FT                   /note="K->A: No effect."
FT                   /evidence="ECO:0000269|PubMed:24236216"
FT   MUTAGEN         104
FT                   /note="W->A: No effect."
FT                   /evidence="ECO:0000269|PubMed:24236216"
FT   MUTAGEN         114
FT                   /note="R->D: No effect."
FT                   /evidence="ECO:0000269|PubMed:24236216"
FT   MUTAGEN         118
FT                   /note="N->A: No effect."
FT                   /evidence="ECO:0000269|PubMed:24236216"
FT   MUTAGEN         187
FT                   /note="D->K: No effect."
FT                   /evidence="ECO:0000269|PubMed:24236216"
SQ   SEQUENCE   371 AA;  42133 MW;  563A742EEABEF171 CRC64;
     MTSLSDILAS SAEAGLSLQR SDGSMPAGHN GPYHDPETPV RNTSHWLVTF LKAHELTDEN
     RFRQAASDAV SYLLSEEARP HGHTFEHRQN DTKDRCNGLM GQAWSLEALA LAARALDNER
     AAAVAADVFL SHPFCDKLKL WQRVDTDGTI LGFDRTFNHQ LWFAASGGLV AHTAPQEVSQ
     RVRDFLDSLP STIDLYENGL IRHPLRPSMD LSELAESVTH DVHRSMVRNH LLHYLRPPRS
     KRRLRNKAEG YHSFNLYALA ILAREFPSHS VWSTDLLSDI LEYTLSEEFR EATTDNKFSH
     PYNPPGFEVP AAMETFSVGS YKEREMWVNE QIQHSFDPNT SLLTRGTDDK QTHAARLYEA
     TRLDDYEIYL D