ID AGLG_HALVO Reviewed; 313 AA. AC B2G4W7; DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot. DT 10-JUN-2008, sequence version 1. DT 16-MAY-2012, entry version 12. DE RecName: Full=Glycosyltransferase AglG; DE EC=2.4.1.-; DE AltName: Full=Archaeal glycosylation protein G; GN Name=aglG; OS Haloferax volcanii (Halobacterium volcanii). OC Archaea; Euryarchaeota; Halobacteria; Halobacteriales; OC Halobacteriaceae; Haloferax. OX NCBI_TaxID=2246; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN GLYCOSYLATION, PATHWAY, RP AND GENE NAME. RC STRAIN=WR536 / H53 / DS70; RX PubMed=18631242; DOI=10.1111/j.1365-2958.2008.06352.x; RA Yurist-Doutsch S., Abu-Qarn M., Battaglia F., Morris H.R., RA Hitchen P.G., Dell A., Eichler J.; RT "AglF, aglG and aglI, novel members of a gene island involved in the RT N-glycosylation of the Haloferax volcanii S-layer glycoprotein."; RL Mol. Microbiol. 69:1234-1245(2008). CC -!- FUNCTION: Involved in N-glycosylation of the S-layer glycoprotein. CC Contributes to the assembly of the pentasaccharide decorating at CC least 2 select Asn residues of the S-layer glycoprotein. CC Contributes to the addition of the hexuronic acid found at CC position 2 of the pentasaccharide. CC -!- PATHWAY: Cell surface structure biogenesis; S-layer biogenesis. CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein CC (Potential). CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. 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; AM991130; CAQ51231.1; -; Genomic_DNA. DR ProteinModelPortal; B2G4W7; -. DR CAZy; GT2; Glycosyltransferase Family 2. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW. DR InterPro; IPR001173; Glyco_trans_2. DR Pfam; PF00535; Glycos_transf_2; 1. PE 1: Evidence at protein level; KW Cell membrane; Glycosyltransferase; Membrane; Transferase; KW Transmembrane; Transmembrane helix. FT CHAIN 1 313 Glycosyltransferase AglG. FT /FTId=PRO_0000415420. FT TRANSMEM 284 304 Helical; (Potential). SQ SEQUENCE 313 AA; 35802 MW; 318704140B04FDF8 CRC64; MKVSVVVCTY SMERYESFSE TVESVLAQTY EPLELVIVVD GNEEEFDRVQ DDFGDIDDVV LHCNDENRGI SYSRTKGAEL GTGDVVAMID DDATAEPDWI ETLVDTYENN PDAVAVGGTV VPDWVARKPE FFPEEFYWLV GCDERGFGEH MEEVRNTYGS NISFKRDVFL EVGGYDTNTG RKGDKHVQAH EAPVCIRIYE QTGERVIYNK QARVNHKLFE YRTEFDWLVF RSFWQGYSKR VMDLLYPQAS DDKNAYLKDL MLVYVVDRLK NLVEDPSLAQ VQQLIAIFVF TAAVGFGYVY GLLTPNLVEK TNN //