Latest update: September 24, 2018


ProGT15 (AglB)

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ProGT ID ProGT15 (AglB)
ProGT Pathway
Organism Information
Organism NameHaloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii)
Clinical ImplicationNon-pathogenic
DomainArchaebacteria
PhylumEuryarchaeota
ClassificationFamily: Halobacteriaceae
Order: Halobacteriales
Class: Halobacteria or Halomebacteria
Division or phylum: "Euryarchaeota"
Taxonomic ID (NCBI)309800
Genome Information
Gene BankCP001956.1
EMBLAM922226
Gene Information
Gene NameaglB
NCBI Gene ID8923906
Protein information
Protein NameAglB 
UniProtKB/ SwissProt IDD4GYH4
NCBI Ref SeqYP_003535577.1
UniProtKB Sequence>sp|D4GYH4|AGLB_HALVD Dolichyl-monophosphooligosaccharide--protein glycotransferase AglB OS=Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) GN=aglB PE=1 SV=1 MSDEQTKYSPSIAELARDWYHIPVLSTIILVMLWIRLRSYDAFIREGTVFFSGNDAWYHL RQVEYTVRNWPATMPFDPWTEFPFGRTAGQFGTIYDQLVATAALVVGLGSPSSDLVAKSL LVAPAVFGALTVIPTYLIGKRLGGRLGGLFGAVILMLLPGTFLQRGLVGFADHNIVEPFF MGFAVLAIMIALTVADREKPVWELVAARDLDALREPLKWSVLAGVATAIYMWSWPPGILL VGIFGLFLVLKMASDYVRGRSPEHTAFVGAISMTVTGLLMFIPIEEPGFGVTDFGFLQPL FSLGVALGAVFLAALARWWESNDVDERYYPAVVGGTMLVGIVLFSLVLPSVFDSIARNFL RTVGFSAGAATRTISEAQPFLAANVLQSNGQTAVGRIMSEYGFTFFTGALAAVWLVAKPL VKGGNSRKIGYAVGSLALIGVLFLIPALPAGIGSALGVEPSLVSLTIVTALIVGAVMQAD YESERLFVLVWAAIITSAAFTQVRFNYYLAVVVAVMNAYLLREALGIDFVGLANVERFDD ISYGQVAAVVIAVLLILTPVLIIPIQLGNGGVSQTAMQASQTGPGTVTQWDGSLTWMQNN TPAEGEFGGESNRMEYYGTYEYTDDFDYPDGAYGVMSWWDYGHWITVLGERIPNANPFQG GATEAANYLLAEDEQQAESVLTSMGDDGEGDQTRYVMVDWQMASTDAKFSAPTVFYDESN ISRSDFYNPMFRLQEQGEQTTVAAASSLKDQRYYESLMVRLYAYHGSAREASPIVVDWEE RTSADGSTTFRVTPSDGQAVRTFDNMSAAEEYVANDPTSQIGGIGTFPEERVSALEHYRL VKSSNSSALRSGSYQRSLISEGNTYGLQPQALVPNNPAWVKTFERVPGATVDGSGAPANT TVTARVQMRDLTTGTNFTYTQQAQTDADGEFTMTLPYSTTGYDEYGPDNGYTNVSVRAAG GYAFTGPTSVTGNSTIVSYQAENVAVDEGLVNGAEDGTVQVTLERNEQELDLPGDSSSED SSSEDGTSDGSQTNESASTSTSASVDASAVSAAA
EMBL CDSCAP58184.1
Sequence length1054 AA
Subcellular LocationMembrane (Integral component of membrane)
Function in Native Organism 1) AglB is OSTase transfer the pentasaccharide to the S-layer protein.
2) For motility of flagella, the presence of the entire pentasaccharide is essential, and for the flagellum assembly requires AglB-dependent glycosylation of FlgA1.
String309800.HVO_1530.
Additional Information1) AglB and AglD are involved in assembly of S-layer glycoproteins.
2) H. volcanii AglB shows a relaxed substrate specificity and can transfer truncated glycan to the S-layer glycoprotein, as in aglD deleted cells, similar OSTs also reported in C. jejuni PglB and AglB from the methanoarchaea M. voltae
Glycosyltransferase Information
Glycosylation TypeN- (Asn) linked 
CAZY FamilyGT66
EC Number (BRENDA)2.4.1.-
Mechanism of Glycan TransferEn bloc
Acceptor specificity Sequon_1Asn-Xaa-Ser
Donor TypeLipid linked sugars
Donor SpecificityDolP-Pentasaccharide
Accessory GT IDProGT15.1 ProGT15.2 ProGT15.3 ProGT15.4 ProGT15.5 ProGT15.6 ProGT15.7 ProGT15.8 ProGT15.9 ProGT15.10 ProGT15.11 ProGT15.12ProGT15.13 ProGT15.14 ProGT15.15 ProGT15.16 ProGT15.17 ProGT1
Glycan Information
Glycan transferredPentasaccharide (2 Monosaccharides (hexose)s, 2 hexuronic acids and a methyl ester of hexuronic acid) 
Method of Glycan IndentificationIn-source collision-induced dissociation (IS-CID), LC-ESI-MS and LC-MS/MS
Experimental_strategiesIn vivo 
Acceptor Subtrate Information
Acceptor Substrate name S-layer glycoprotein
ProGPdb ID ProGP71
Acceptor Substrate name PilA1
ProGPdb ID ProGP545
Acceptor Substrate name PilA2
ProGPdb ID ProGP546
Acceptor Substrate name PilA3
ProGPdb ID ProGP547
Acceptor Substrate name PilA4
ProGPdb ID ProGP548
Acceptor Substrate name PilA6
ProGPdb ID ProGP549
Acceptor Substrate name FlgA1
ProGPdb ID ProGP543
Acceptor Substrate name FlgA2
ProGPdb ID ProGP544
Litrature
Year Of Validation2006 
Reference Abu-Qarn, M., & Eichler, J. (2006). Protein N-glycosylation in Archaea: defining Haloferax volcanii genes involved in S-layer glycoprotein glycosylation. Molecular microbiology, 61(2), 511-525.

Authors Abu-Qarn, M., & Eichler, J.
Research groupsDepartment of Life Sciences, Ben Gurion University, Beersheva 84105, Israel.
Corresponding Author Eichler, J.
ContactsDepartment of Life Sciences, Ben Gurion University, Beersheva 84105, Israel.
Reference Yurist-Doutsch, S., Abu-Qarn, M., Battaglia, F., Morris, H. R., Hitchen, P. G., Dell, A., & Eichler, J. (2008). aglF, aglG and aglI, novel members of a gene island involved in the N-glycosylation of the Haloferax volcanii S-layer glycoprotein. Molecular microbiology, 69(5), 1234-1245.-

Authors Yurist-Doutsch, S., Abu-Qarn, M., Battaglia, F., Morris, H. R., Hitchen, P. G., Dell, A., & Eichler, J.
Research groupsDepartment of Life Sciences, Ben Gurion University, Beersheva 84105, Israel.
Corresponding Author Eichler, J.
ContactsDepartment of Life Sciences, Ben Gurion University, Beersheva 84105, Israel.
Reference Kaminski, L., Abu-Qarn, M., Guan, Z., Naparstek, S., Ventura, V.V., Raetz, C.R., Hitchen, P.G., Dell, A. & Eichler, J. (2010). AglJ adds the first sugar of the N-linked pentasaccharide decorating the Haloferax volcanii S-layer glycoprotein. Journal of bacteriology, 192(21), 5572-5579.

Authors Kaminski, L., Abu-Qarn, M., Guan, Z., Naparstek, S., Ventura, V.V., Raetz, C.R., Hitchen, P.G., Dell, A. & Eichler, J.
Research groupsDepartment of Life Sciences, Ben Gurion University, Beersheva 84105, Israel.
Corresponding Author Eichler, J.
ContactsDepartment of Life Sciences, Ben Gurion University, Beersheva 84105, Israel.
Reference Yurist-Doutsch, S., Magidovich, H., Ventura, V. V., Hitchen, P. G., Dell, A., & Eichler, J. (2010). N-glycosylation in Archaea: on the coordinated actions of Haloferax volcanii AglF and AglM. Molecular microbiology, 75(4), 1047-1058.

Authors Yurist-Doutsch, S., Magidovich, H., Ventura, V. V., Hitchen, P. G., Dell, A., & Eichler, J.
Research groupsDepartment of Life Sciences, Ben Gurion University, Beersheva 84105, Israel.
Corresponding Author Eichler, J.
ContactsDepartment of Life Sciences, Ben Gurion University, Beersheva 84105, Israel.
Reference Cohen-Rosenzweig, C., Yurist-Doutsch, S., & Eichler, J. (2012). AglS, a novel component of the Haloferax volcanii N-glycosylation pathway, is a dolichol phosphate-mannose mannosyltransferase. Journal of bacteriology, JB-01716.

Authors Cohen-Rosenzweig, C., Yurist-Doutsch, S., & Eichler, J.
Research groupsDepartment of Life Sciences, Ben Gurion University, Beersheva 84105, Israel.
Corresponding Author Eichler, J.
ContactsDepartment of Life Sciences, Ben Gurion University, Beersheva 84105, Israel.
Reference Kaminski, L., Guan, Z., Abu-Qarn, M., Konrad, Z., & Eichler, J. (2012). AglR is required for addition of the final mannose residue of the N-linked glycan decorating the Haloferax volcanii S-layer glycoprotein. Biochimica et Biophysica Acta (BBA)-General Subjects, 1820(10), 1664-1670.

Authors Kaminski, L., Guan, Z., Abu-Qarn, M., Konrad, Z., & Eichler, J.
Research groupsDepartment of Life Sciences, Ben Gurion University, Beersheva 84105, Israel.
Corresponding Author Eichler, J.
ContactsDepartment of Life Sciences, Ben Gurion University, Beersheva 84105, Israel.
Reference Tripepi, M., You, J., Temel, S., Önder, Ö., Brisson, D., & Pohlschröder, M. (2012). N-glycosylation of Haloferax volcanii flagellins requires known Agl proteins and is essential for biosynthesis of stable flagella. Journal of bacteriology, JB-00731.

Authors Tripepi, M., You, J., Temel, S., Önder, Ö., Brisson, D., & Pohlschröder, M.
Research groupsDepartment of Biology, University of Pennsylvania, Philadelphia, Pennsylvania, USA
Corresponding Author Pohlschröder, M.
ContactsDepartment of Biology, University of Pennsylvania, Philadelphia, Pennsylvania, USA
Reference Arbiv, A., Yurist-Doutsch, S., Guan, Z., & Eichler, J. (2013). AglQ is a novel component of the Haloferax volcanii N-glycosylation pathway. PLoS One, 8(11), e81782.

Authors Arbiv, A., Yurist-Doutsch, S., Guan, Z., & Eichler, J.
Research groupsDepartment of Life Sciences, Ben Gurion University, Beersheva 84105, Israel.
Corresponding AuthorEichler, J.
ContactsDepartment of Life Sciences, Ben Gurion University, Beersheva 84105, Israel.
Reference Abu-Qarn, M., Yurist-Doutsch, S., Giordano, A., Trauner, A., Morris, H.R., Hitchen, P., Medalia, O., Dell, A.. & Eichler, J. (2007). Haloferax volcanii AglB and AglD are involved in N-glycosylation of the S-layer glycoprotein and proper assembly of the surface layer. Journal of molecular biology, 374(5), 1224-1236.

Authors Abu-Qarn, M., Yurist-Doutsch, S., Giordano, A., Trauner, A., Morris, H.R., Hitchen, P., Medalia, O., Dell, A.. & Eichler, J.
Research groupsDepartment of Life Sciences, Ben Gurion University, Beersheva 84105, Israel.
Corresponding AuthorEichler, J.
ContactsDepartment of Life Sciences, Ben Gurion University, Beersheva 84105, Israel.
Reference Kaminski, L., Guan, Z., Yurist-Doutsch, S., & Eichler, J. (2013). Two distinct N-glycosylation pathways process the Haloferax volcanii S-layer glycoprotein upon changes in environmental salinity. MBio, 4(6), e00716-13.

Authors Kaminski, L., Guan, Z., Yurist-Doutsch, S., & Eichler, J.
Research groupsDepartment of Life Sciences, Ben Gurion University, Beersheva 84105, Israel.
Corresponding AuthorEichler, J.
ContactsDepartment of Life Sciences, Ben Gurion University, Beersheva 84105, Israel.
Reference Esquivel, R. N., Schulze, S., Hippler, M., & Pohlschroder, M. (2016). Identification of Haloferax volcanii pilin N-glycans with diverse roles in pilus-biosynthesis, adhesion and microcolony formation. Journal of Biological Chemistry, jbc-M115.

Authors Esquivel, R. N., Schulze, S., Hippler, M., & Pohlschroder, M.
Research groupsDepartment of Biology, University of Pennsylvania, Philadelphia, Pennsylvania, USA
Corresponding AuthorPohlschroder, M.
ContactsDepartment of Biology, University of Pennsylvania, Philadelphia, Pennsylvania, USA