AGL15_HALVD
ID AGL15_HALVD Reviewed; 472 AA.
AC D4GU68;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 25-MAY-2022, entry version 52.
DE RecName: Full=Probable low-salt glycan biosynthesis flippase Agl15;
GN Name=agl15; OrderedLocusNames=HVO_2055; ORFNames=C498_05558;
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 FUNCTION, PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=24194539; DOI=10.1128/mbio.00716-13;
RA Kaminski L., Guan Z., Yurist-Doutsch S., Eichler J.;
RT "Two distinct N-glycosylation pathways process the Haloferax volcanii S-
RT layer glycoprotein upon changes in environmental salinity.";
RL MBio 4:E00716-E00716(2013).
CC -!- FUNCTION: Flippase involved in N-glycan biosynthetic pathway that takes
CC place under low-salt conditions (1.75 M instead of 3.4 M). Participates
CC in the formation of the tetrasaccharide present at 'Asn-532' of S-layer
CC glycoprotein Csg, consisting of a sulfated hexose, 2 hexoses and
CC rhamnose. Probably moves the tetrasaccharide from the cytosolic to the
CC extracytosolic side of the membrane. {ECO:0000269|PubMed:24194539}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:24194539}.
CC -!- PATHWAY: Cell surface structure biogenesis; S-layer biogenesis.
CC {ECO:0000269|PubMed:24194539}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Impaired formation of the tetrasaccharide present
CC at 'Asn-532' of S-layer glycoprotein Csg. The complete tetrasaccharide
CC is formed but does not make it to the S-layer glycoprotein Csg. No
CC effect on 'Asn-47' and 'Asn-117' glycosylation of S-layer glycoprotein
CC Csg. {ECO:0000269|PubMed:24194539}.
CC -!- SIMILARITY: Belongs to the AglR/Agl15 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; CP001956; ADE05104.1; -; Genomic_DNA.
DR EMBL; AOHU01000040; ELY33648.1; -; Genomic_DNA.
DR AlphaFoldDB; D4GU68; -.
DR SMR; D4GU68; -.
DR STRING; 309800.C498_05558; -.
DR EnsemblBacteria; ADE05104; ADE05104; HVO_2055.
DR EnsemblBacteria; ELY33648; ELY33648; C498_05558.
DR KEGG; hvo:HVO_2055; -.
DR PATRIC; fig|309800.29.peg.1078; -.
DR eggNOG; arCOG02209; Archaea.
DR HOGENOM; CLU_043240_0_0_2; -.
DR OMA; FYSWMDV; -.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
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 3: Inferred from homology;
KW Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..472
FT /note="Probable low-salt glycan biosynthesis flippase
FT Agl15"
FT /id="PRO_0000428766"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 408..428
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 434..454
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 472 AA; 51165 MW; 5C56C28ED2A3E6F7 CRC64;
MDLARSSIKL FIANIFGAGL QFLGITFFAR ELGASQMGVF FLFQALLGIV AIPADFGLRG
AVEKRISEGI QPGEYLSSAI ILKLIPISLI ILSIVVFEQR INGYLGGDFA VYLALAIILQ
ETAQLAVSVL KGELRVGETA ELNIIRRITW VGGGFLLVSS GLDAEALIYS LLAGMVVTLA
WGLSKISTSL KKPSFKNARS LFNYSKYSVV SSIGGYFYSW MDVAIIGIFL TQSHVGAYET
AWRVTAITML FSQAVASTIF PQVSQWSSKN EQQQIESVIS NSITPSMLLV IPAFFGILVF
SDEIMGIVFG SEFTIASYVL IILAGEKILQ SVHVIIGRSL QALNQPGLAA RATVISVVLN
LILNVILILS FGIVGAAVAT ALSFAVNTVL HAHYLSSFVS IKFQYSQIGW CTVSSLIMAG
VLFGFKTLVG VNSLIQLFIG IFFGMLVYTT ITLLYQPIRE TAFKNLIRLV PI
