AGLS_HALVD
ID AGLS_HALVD Reviewed; 457 AA.
AC D4GYH0;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Dolichol phosphate-mannose mannosyltransferase {ECO:0000303|PubMed:23086206};
DE EC=2.4.1.- {ECO:0000305|PubMed:23086206};
DE AltName: Full=Archaeal glycosylation protein S;
GN Name=aglS; OrderedLocusNames=HVO_1526; ORFNames=C498_02985;
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 [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 [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=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 [3]
RP PROBABLE FUNCTION IN GLYCOSYLATION OF FLAGELLINS.
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).
RN [4]
RP FUNCTION, PATHWAY, SUBCELLULAR LOCATION, TOPOLOGY, DISRUPTION PHENOTYPE,
RP AND GENE NAME.
RC STRAIN=H53;
RX PubMed=23086206; DOI=10.1128/jb.01716-12;
RA Cohen-Rosenzweig C., Yurist-Doutsch S., Eichler J.;
RT "AglS, a novel component of the Haloferax volcanii N-glycosylation pathway,
RT is a dolichol phosphate-mannose mannosyltransferase.";
RL J. Bacteriol. 194:6909-6916(2012).
CC -!- FUNCTION: Involved in the assembly of a N-linked pentasaccharide that
CC decorates the S-layer glycoprotein and flagellins. Transfers mannose,
CC the terminal pentasaccharide residue, from its dedicated dolichol
CC phosphate carrier to the protein-bound glycan comprising the first four
CC subunits of the N-linked pentasaccharide.
CC {ECO:0000269|PubMed:23086206}.
CC -!- PATHWAY: Cell surface structure biogenesis; S-layer biogenesis.
CC {ECO:0000269|PubMed:23086206}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:23086206}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23086206};
CC Multi-pass membrane protein {ECO:0000269|PubMed:23086206}.
CC -!- DISRUPTION PHENOTYPE: Mutants lack the final mannose subunit of the N-
CC linked pentasaccharide. {ECO:0000269|PubMed:23086206}.
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DR EMBL; CP001956; ADE02987.1; -; Genomic_DNA.
DR EMBL; AOHU01000028; ELY35751.1; -; Genomic_DNA.
DR AlphaFoldDB; D4GYH0; -.
DR STRING; 309800.C498_02985; -.
DR EnsemblBacteria; ADE02987; ADE02987; HVO_1526.
DR EnsemblBacteria; ELY35751; ELY35751; C498_02985.
DR KEGG; hvo:HVO_1526; -.
DR PATRIC; fig|309800.29.peg.573; -.
DR eggNOG; arCOG02043; Archaea.
DR HOGENOM; CLU_607814_0_0_2; -.
DR OMA; PSTCHYR; -.
DR BioCyc; MetaCyc:MON-19289; -.
DR BRENDA; 2.4.1.B58; 2561.
DR UniPathway; UPA00378; -.
DR UniPathway; UPA00977; -.
DR Proteomes; UP000008243; Chromosome.
DR Proteomes; UP000011532; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:CACAO.
DR GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IDA:CACAO.
DR GO; GO:0045232; P:S-layer organization; IEA:UniProtKB-UniPathway.
DR InterPro; IPR031897; AglS.
DR Pfam; PF15971; Mannosyl_trans4; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycosyltransferase; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..457
FT /note="Dolichol phosphate-mannose mannosyltransferase"
FT /id="PRO_0000422306"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..91
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..120
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..173
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..211
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 233..259
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 281..283
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 305..307
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 329..337
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 359..457
FT /note="Extracellular"
FT /evidence="ECO:0000255"
SQ SEQUENCE 457 AA; 50656 MW; F8D74C2E874756BE CRC64;
MKRLAKAAFS QNSLTAPIVS TFVYLISVVR VVLNGNWPVT SSDTAMFQHI GWMVFSGKRY
YIDAWDPKPP LTLELATIIA YISNGDPHLQ HTLSVVSTIV AGILLTYLIS HITSEITGNQ
FAGLLSGIVF ITFPVIHYSA VFGYEPKYFV FLFGLGSIYL SRNPKPILSG AAAAASAGMW
QFAIIFPIIS FGIISRRKSK DLILKYVFGA TIIAFISLLP IYLQGGLVAM TVEVIIAPLY
AGETQSFLYR LVKGVTHLKL MIPIALLGMA GILLGFLDDI RERWWVVGLL LWFCIQIFIL
DYDGADDLFL GIILVSMGIG FAFEKLSTKY ESERINSIVT AVVVCMLIWQ VVTLGGVGVI
TNPYSYSGDG PDQAILESGI QQFAHLSGYT EYTIGGSPPD EQYNVKSRYG PDKIEELFFT
STIPSTCHYR LSGMELEWMN LTEQSFTEEK CGKWRLP
