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Literature summary for 2.4.99.21 extracted from

  • Abu-Qarn, M.; Yurist-Doutsch, S.; Giordano, A.; Trauner, A.; Morris, H.R.; Hitchen, P.; Medalia, O.; Dell, A.; Eichler, J.
    Haloferax volcanii AglB and AglD are involved in N-glycosylation of the S-layer glycoprotein and proper assembly of the surface layer (2007), J. Mol. Biol., 374, 1224-1236.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Haloferax volcanii D4GYH4
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Haloferax volcanii DSM 3757 D4GYH4
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Synonyms

Synonyms Comment Organism
AlgB
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Haloferax volcanii

General Information

General Information Comment Organism
physiological function cells lacking glycotransferase AglB are unable to N-glycosylate the S-layer glycoprotein. The absence of AglB results in enhanced release of the S-layer glycoprotein. Haloferax volcanii AglB mutant cells grow significantly less well at elevated salt levels than do cells of the background strain Haloferax volcanii