ArticleJournal of bacteriology2012
The accessory Sec protein Asp2 modulates GlcNAc deposition onto the serine-rich repeat glycoprotein GspB.
Article in Journal of bacteriology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 28 citations in OpenAlex.
- Genome co-adaptation and the evolution of methicillin resistant Staphylococcus aureus.Genome biology · 2026Article
- Serine-rich repeat proteins: well-known yet little-understood bacterial adhesins.Journal of bacteriology · 2024Review
- Serine-rich repeat proteins from gut microbes.Gut microbes · 2020Review
- Streptococcal Serine-Rich Repeat Proteins in Colonization and Disease.Frontiers in microbiology · 2020Review
- Recognition of specific sialoglycan structures by oral streptococci impacts the severity of endocardial infection.PLoS pathogens · 2019Article
- Membrane trafficking of the bacterial adhesin GspB and the accessory Sec transport machinery.The Journal of biological chemistry · 2019Article
- Serine-rich repeat protein adhesins from Lactobacillus reuteri display strain specific glycosylation profiles.Glycobiology · 2019Article
- Biology of Oral Streptococci.Microbiology spectrum · 2018Review
- Carb loading takes proteins on a ride.The Journal of biological chemistry · 2018Article
- O-acetylation of the serine-rich repeat glycoprotein GspB is coordinated with accessory Sec transport.PLoS pathogens · 2017Article
- Transcriptional organization of pneumococcal psrP-secY2A2 and impact of GtfA and GtfB deletion on PsrP-associated virulence properties.Microbes and infection · 2017Article
- Defining the enzymatic pathway for polymorphicThe Journal of biological chemistry · 2017Article
- The Plasmin-Sensitive Protein Pls in Methicillin-Resistant Staphylococcus aureus (MRSA) Is a Glycoprotein.PLoS pathogens · 2017Article
- Emerging facets of prokaryotic glycosylation.FEMS microbiology reviews · 2017Review
- The sweet tooth of bacteria: common themes in bacterial glycoconjugates.Microbiology and molecular biology reviews : MMBR · 2014Review
- Selective transport by SecA2: an expanding family of customized motor proteins.Biochimica et biophysica acta · 2014Review
- Both GtfA and GtfB are required for SraP glycosylation in Staphylococcus aureus.Current microbiology · 2014Article
- Structure of a novel O-linked N-acetyl-D-glucosamine (O-GlcNAc) transferase, GtfA, reveals insights into the glycosylation of pneumococcal serine-rich repeat adhesins.The Journal of biological chemistry · 2014Article
- Gap2 promotes the formation of a stable protein complex required for mature Fap1 biogenesis.Journal of bacteriology · 2013Article
- Differential localization of the streptococcal accessory sec components and implications for substrate export.Journal of bacteriology · 2013Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The accessory Sec system is a specialized transport system that exports serine-rich repeat (SRR) glycoproteins of Gram-positive bacteria. This system contains two homologues of the general secretory (Sec) pathway (SecA2 and SecY2) and several other essential proteins (Asp1 to Asp5) that share no homology to proteins of known function. In Streptococcus gordonii, Asp2 is required for the transport of the SRR adhesin GspB, but its role in export is unknown. Tertiary structure predictions suggest that the carboxyl terminus of Asp2 resembles the catalytic region of numerous enzymes that function through a Ser-Asp-His catalytic triad. Sequence alignment of all Asp2 homologues identified a highly conserved pentapeptide motif (Gly-X-Ser(362)-X-Gly) typical of most Ser-Asp-His catalytic triads, where Ser forms the reactive residue. Site-directed mutagenesis of residues comprising the predicted catalytic triad of Asp2 of S. gordonii had no effect upon GspB transport but did result in a marked change in the electrophoretic mobility of the protein. Lectin-binding studies and monosaccharide content analysis of this altered glycoform revealed an increase in glucosamine deposition. Random mutagenesis of the Asp2 region containing this catalytic domain also disrupted GspB transport. Collectively, our findings suggest that Asp2 is a bifunctional protein that is essential for both GspB transport and correct glycosylation. The catalytic domain may be responsible for controlling the glycosylation of GspB, while other surrounding regions are functionally required for glycoprotein transport.
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