ID   AGLP_HALVD              Reviewed;         239 AA.
AC   D4GYG5; B7VU77;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Hexuronic acid methyltransferase AglP;
DE            EC=2.1.1.-;
DE   AltName: Full=Archaeal glycosylation protein P;
GN   Name=aglP; OrderedLocusNames=HVO_1522;
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   FUNCTION AS A METHYLTRANSFERASE, PATHWAY, AND SUBCELLULAR LOCATION.
RC   STRAIN=DS2 / DS70;
RX   PubMed=20149102; DOI=10.1111/j.1365-2958.2010.07090.x;
RA   Magidovich H., Yurist-Doutsch S., Konrad Z., Ventura V.V., Dell A.,
RA   Hitchen P.G., Eichler J.;
RT   "AglP is a S-adenosyl-L-methionine-dependent methyltransferase that
RT   participates in the N-glycosylation pathway of Haloferax volcanii.";
RL   Mol. Microbiol. 76:190-199(2010).
RN   [4]
RP   FUNCTION.
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   [5]
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. S-adenosyl-L-
CC       methionine-dependent methyltransferase that modifies the hexuronic acid
CC       found at position 4 of the pentasaccharide.
CC       {ECO:0000269|PubMed:20149102, ECO:0000269|PubMed:21091511,
CC       ECO:0000269|PubMed:22730124}.
CC   -!- PATHWAY: Cell surface structure biogenesis; S-layer biogenesis.
CC       {ECO:0000269|PubMed:20149102}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20149102}.
CC   -!- DISRUPTION PHENOTYPE: Mutants exhibit defective or limited motility.
CC       {ECO:0000269|PubMed:22730124}.
CC   -!- SIMILARITY: Belongs to the FkbM methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; FM955369; CAW30727.1; -; Genomic_DNA.
DR   EMBL; CP001956; ADE04550.1; -; Genomic_DNA.
DR   AlphaFoldDB; D4GYG5; -.
DR   SMR; D4GYG5; -.
DR   STRING; 309800.C498_02960; -.
DR   EnsemblBacteria; ADE04550; ADE04550; HVO_1522.
DR   KEGG; hvo:HVO_1522; -.
DR   eggNOG; arCOG01402; Archaea.
DR   HOGENOM; CLU_081183_0_0_2; -.
DR   OMA; WQYERFR; -.
DR   BioCyc; MetaCyc:MON-19287; -.
DR   UniPathway; UPA00977; -.
DR   Proteomes; UP000008243; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0045232; P:S-layer organization; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR006342; FkbM_mtfrase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF05050; Methyltransf_21; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR01444; fkbM_fam; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Methyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..239
FT                   /note="Hexuronic acid methyltransferase AglP"
FT                   /id="PRO_0000415367"
SQ   SEQUENCE   239 AA;  26263 MW;  228668C62FF4B596 CRC64;
     MTIVKKVARL RDWIALKTGA IRSPMIAEVS GYAARFTVQS VEEIWRIRDL RGEQDVIRLL
     LEEAEEDDVL WDVGSNIGTH ACICSTKANV FAFEPNPDTF DRLTENSDRA PGTVIPLRYG
     LSSSSGDISF EPSPIAANGT HKVSTEGSMT IKTISGDELV ESGEVPKPNV VKVDVEGHEL
     EVLKGMTNAL QSVNFVIVEI HAGVDPKDVT KLLSEAKLST EITKLNRDED FVIGRRQND