ProGT51 (AglB)

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ProGT ID ProGT51 (AglB)
Organism Information
Organism NameSulfolobus acidocaldarius
Clinical ImplicationNon-pathogenic
DomainArchaebacteria
Classification Phylum : Crenarchaeota
Class : Thermoprotei
Orders : Sulfolobales
Family : Sulfolobaceae
Genus : Sulfolobus
Species : acidocaldarius
Taxonomic ID (NCBI)330779 
Genome Information
Gene BankCP000077.1
EMBLCP000077 
Gene Information
Gene Namesaci1274
NCBI Gene ID3473075
NCBI Reference SequenceNC_007181.1.
Protein information
Protein NameAglB 
UniProtKB/ SwissProt IDQ4J9B4
NCBI Ref SeqWP_011278118.1
UniProtKB Sequence>tr|Q4J9B4|Q4J9B4_SULAC Conserved membrane protein OS=Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770) GN=Saci_1274 PE=4 SV=1 MQSTSILARIDKFKFLDAIIIGSLALFSILIRIISITAFPQTINGFDSWYLFYNALLIVK AGGNWYAVPPDVHAWFPWGYFIELENTIGLPFLVALFSVPFYSIFGQNIVYTLTLVSPIV LDGIGVVAAFLAVESITNSRVGGYIAAAITAFTPSLTYKNILGSLPKTSWGGVFVLFTIY FLSLAIKKKKPLYGIPAGIMIFLANITWGGYTYIDISLAIAAFLIVLFNKNDEISAKTLT ISGITAAFLTSLSPNTIGFMSEVAHGLALLIIPLFLYLDLYLRRVLPKDIVDSKNIVIGA AIILLVSLVVLGSVAFKVQLIPSRYYAIINPFFQFTVPIDRTVAEYIPQSIAAMIQDFGI GLFLSIIGIYFLLTRKQDMAGIWLVVLGAASIYGTSEQPYLFNYTIYIVAALAGVAVAEL FSRFMERKIRIAPILMLTLIGVALLADAGIAVEASYAPQALINSSTSYLTTNYAWISALD WINQNTPNNAFILSWWDYGYWIHAVGNRTVIDENNTLNGTQIKLMAEMFLNNESFAVNVL ENDFHLYPYGNPNYTRPVYIVAYDAVTEYIVNNQYPVWFIGYPTNFPGTFIGYTTSLGDI AKAIGAMTTIAGYNTNSYVNTTYINETASYAAQYNSQLASIIANSLPMAWTPKTYNSLIG SMFIEAIQSLNQGPVQAPFSISLSQLLQSSSTSLYNPNALLPRVNLMYFKPVYIALFPLS VTNALGGEAIVYIMVYIYQFVMPNVIIPPTISTA
EMBL CDSAAY80616.1
Sequence length754 AA
Subcellular LocationMembrane (Integral component of membrane)
Function in Native Organism 1) The composition of SlaA glycan is changed in the ?agl3 deletion mutant, this significantly reduces the growth rate at elevated salt concentrations.
String330779.Saci_1274
Additional Information1) AglB catalyzes the final step of the transfer of glycan to S-layer protein as well as to other surface exposed proteins.
Glycosyltransferase Information
Glycosylation TypeN- (Asn) linked 
CAZY FamilyGT66
EC Number (BRENDA)2.4.99.18 6160
Mechanism of Glycan TransferEn bloc
Accessory GT IDProGT51.1, ProGT51.2, ProGT51.3
Glycan Information
Glycan transferredHexasaccharide (Glc1Man2GlcNAc2QuiS)  
Method of Glycan IndentificationMALDI-MS, NMR, and nanoLC ES-MS/MS
Experimental_strategiesIn vivo and In vitro 
Acceptor Subtrate Information
Acceptor Substrate name Cytochrome b558/566 subunit A
ProGPdb ID ProGP150
Acceptor Substrate name SlaA (S- layer protein)
ProGPdb ID ProGP344
Acceptor Substrate name FlaB
Litrature
Year Of Validation2011 
Reference Meyer, B.H., Zolghadr, B., Peyfoon, E., Pabst, M., Panico, M., Morris, H.R., Haslam, S.M., Messner, P., Schäffer, C., Dell, A. and Albers, S.V., 2011. Sulfoquinovose synthase–an important enzyme in the N?glycosylation pathway of Sulfolobus acidocaldarius. Molecular microbiology, 82(5), pp.1150-1163.

Corresponding AuthorMolecular Biology of Archaea, Max-Planck Institute for Terrestrial Microbiology, Marburg, Germany.
Reference Meyer, B.H., Peyfoon, E., Dietrich, C., Hitchen, P., Panico, M., Morris, H.R., Dell, A. and Albers, S.V., 2013. Agl16, a thermophilic glycosyltransferase mediating the last step of N-glycan biosynthesis in the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius. Journal of bacteriology, 195(10), pp.2177-2186.

Corresponding AuthorMolecular Biology of Archaea, Max-Planck Institute for Terrestrial Microbiology, Marburg, Germany.
Reference Meyer, B.H. and Albers, S.V., 2014. AglB, catalyzing the oligosaccharyl transferase step of the archaeal N?glycosylation process, is essential in the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius. Microbiologyopen, 3(4), pp.531-543.

Corresponding AuthorMolecular Biology of Archaea, Max-Planck Institute for terrestrial Microbiology, Karl-von-Frisch-Strasse 10, 35043, Marburg.
Reference Meyer, B.H., Shams-Eldin, H. and Albers, S.V., 2017. AglH, a thermophilic UDP-N-acetylglucosamine-1-phosphate: dolichyl phosphate GlcNAc-1-phosphotransferase initiating protein N-glycosylation pathway in Sulfolobus acidocaldarius, is capable of complementing the eukaryal Alg7. Extremophiles, 21(1), pp.121-134.

Corresponding AuthorMolecular Biology of Archaea, Institute of Biology, University of Freiburg, Schaenzlestrasse 1, 79211, Freiburg, Germany.