AGLR_HALVD
ID AGLR_HALVD Reviewed; 476 AA.
AC D4GYG8; B7VU79;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 25-MAY-2022, entry version 51.
DE RecName: Full=Probable flippase AglR;
DE AltName: Full=Archaeal glycosylation protein R;
GN Name=aglR; OrderedLocusNames=HVO_1524; ORFNames=C498_02975;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 66-476, 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 [4]
RP FUNCTION, PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=H53;
RX PubMed=22750201; DOI=10.1016/j.bbagen.2012.06.014;
RA Kaminski L., Guan Z., Abu-Qarn M., Konrad Z., Eichler J.;
RT "AglR is required for addition of the final mannose residue of the N-linked
RT glycan decorating the Haloferax volcanii S-layer glycoprotein.";
RL Biochim. Biophys. Acta 1820:1664-1670(2012).
RN [5]
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).
CC -!- FUNCTION: Involved in the assembly of a N-linked pentasaccharide that
CC decorates the S-layer glycoprotein and flagellins. Probably mediates or
CC contributes to the translocation of the dolichol-phosphate-mannose
CC across the membrane. {ECO:0000269|PubMed:22750201}.
CC -!- PATHWAY: Cell surface structure biogenesis; S-layer biogenesis.
CC {ECO:0000269|PubMed:22750201}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Mutants show accumulation of both
CC tetrasaccharide- and mannose-linked dolichol phosphate. The final
CC mannose residue of the N-linked glycan decorating the S-layer
CC glycoprotein is not added. {ECO:0000269|PubMed:22750201}.
CC -!- SIMILARITY: Belongs to the AglR/Agl15 family. {ECO:0000305}.
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DR EMBL; CP001956; ADE03191.1; -; Genomic_DNA.
DR EMBL; AOHU01000027; ELY35859.1; -; Genomic_DNA.
DR EMBL; FM955371; CAW30729.1; -; Genomic_DNA.
DR AlphaFoldDB; D4GYG8; -.
DR SMR; D4GYG8; -.
DR STRING; 309800.C498_02975; -.
DR EnsemblBacteria; ADE03191; ADE03191; HVO_1524.
DR EnsemblBacteria; ELY35859; ELY35859; C498_02975.
DR KEGG; hvo:HVO_1524; -.
DR PATRIC; fig|309800.29.peg.571; -.
DR eggNOG; arCOG02209; Archaea.
DR HOGENOM; CLU_043240_0_0_2; -.
DR OMA; VAITFRA; -.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0045232; P:S-layer organization; IEA:UniProtKB-UniPathway.
DR InterPro; IPR029303; Polysacc_synt_C.
DR Pfam; PF14667; Polysacc_synt_C; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..476
FT /note="Probable flippase AglR"
FT /id="PRO_0000422305"
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..373
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..396
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 439..459
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 476 AA; 50636 MW; F2F4AE40E3C963AE CRC64;
MAKLARASAL QFGANVTQTF VGAIITIYVI NELGVGAFGI FALSAALVKW ASIPAVGIRG
AVITRMNESD DISPSEYFTT ASVLTGAIIL VGLLALLGYS PFVEQYLDYS GTQLVGGMFV
SNVSFRLVLG GLRGENRVEM SSLYEALWGI LSSLVKLALV YTGVGVDALF YGEITSSIVI
GIFGVYSLNI SFVSPTRSAA ISLYSWARYG WLDNLKRMSY SWLDTIILGF FVSTSLVGIY
EVAWRISALF VLLPTAISKS TFPTISSLRD TDKLNKVRRI LTRGLSVAGV LAIPGLVGSV
LVGGDILALY GPSVSSVGVA VSVLVSLSVV RLVECYETLV MQALNALDLP DRTFRIGVIF
ITTNIILNVS LIPMFGVIGA AIATLLSMTL GSILAVRALP KAVQTLPPVS AIGSQFVSAG
AMAVVLFTIL NYRPIGQPIE VVLYVLAGAT TYGFVLLSLS SNFRERVQQL LSESLG
