ProGP237 (SgtA)
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| ProGP ID | ProGP237 (SgtA) |
| Validation Status | Characterized |
| Organism Information | |
| Organism Name | Geobacillus tepidamans GS5-97T |
| Domain | Bacteria |
| Classification | Phylum : Firmicutes Class : Bacilli Orders : Bacillales Family : Bacillaceae Genus : Geobacillus Species : tepidamans Strain : GS5-97T |
| Taxonomic ID (NCBI) | 265948 |
| Genome Information | |
| GenBank | AY883421 |
| EMBL | AY883421 |
| Gene Information | |
| Gene Name | sgtA |
| Protein Information | |
| Protein Name | SgtA |
| UniProtKB/SwissProt ID | Q58R21 |
| EMBL-CDS | AAX46285.1 |
| UniProtKB Sequence | >tr|Q58R21|Q58R21_9BACI SgtA OS=Geobacillus tepidamans GN=sgtA PE=4 SV=1 MSKKKAIKLATASAIAASAFVAANPNASEAATNVDAVVSQAKAQMRNAYYTYSHTVTNTG EFADIKAVYAEYNKAKKAYADAVALVKKAGGANKDAYLADLEATYEVYITSRVIPYIDAY NYAVKLDAMRQELQAAVDAKDLAKVEELYHKISYELKSRTVILDRVYGQTTRDLLRSQFK AAAQQLRDSLIYDVTVSMKLKAAEEATNKGDLAAAEKALAEAQDALTKATAFKADLTTKQ ATVKAAYEAKVAPAVVGVSAVNSRTVQIKFNKPIDASTVLVDKGTTDTSDDTLKTTSIVF TALDGQPAISQTDIKASLSDDKKTLTLVAANSDFFTKRYVVDIKNVKTTDGKDVPAYTTT IDTTDSVRPAVLSYSYADNGLTLKVKFSEPLNSVGTVKLYDGTTEISVSPSFTAGSDEMT INLASSSVPVNKALTLKIFGAVDYNGNVINPNPAELTVMKTTVDTTKPTVQSVEAVNDKT VKVTFSEKLLGNPTIKIGGTTAASVSVDSTGLVYTATLNSAQLGIQAVEVSSYTDLAGNV GDAYTKVVELKADTTAPKLVSSQVVKINGIENLVLTFDEEVTTQNNITVVSSNDYYVDEN NVRKQVGVTLTTNSTNFKLYNPVNGKSKSVALDISSLPKGTYTVTLPTGATALVKDLASN PNAYAEGKQITFVRGTDSLTTKPALDTNVSTNGVEVVDNNTLRFTFTQNLDASALNLSNF NINGVALSKAVFDGATNKILVTLAPGANTWTGTHVITVSNIKNVSGIAMDTVTTTESMNE NVAPTFTATLTSADVIKVTFSEPVAHSTLSNAITGNNFTVKVDGTLNNVTGVYTDSAATT PVSATGNTGYKTVYLKLATPVTDLTKPITVSATNLVDVSAEGASPTVVGNTVSSDVVNVA K |
| Sequence length | 901 AA |
| Subcellular Location | Surface |
| Function | Surface layer glycoprotein |
| Glycosylation Status | |
| Glycosylation Type | O- (Ser) linked |
| Experimentally Validated Glycosite(s) in Full Length Protein | S792 |
| Experimentally Validated Glycosite(s ) in Mature Protein | S792 |
| Glycosite(s) Annotated Protein Sequence | >tr|Q58R21|Q58R21_9BACI SgtA OS=Geobacillus tepidamans GN=sgtA PE=4 SV=1 MSKKKAIKLATASAIAASAFVAANPNASEAATNVDAVVSQAKAQMRNAYYTYSHTVTNTG EFADIKAVYAEYNKAKKAYADAVALVKKAGGANKDAYLADLEATYEVYITSRVIPYIDAY NYAVKLDAMRQELQAAVDAKDLAKVEELYHKISYELKSRTVILDRVYGQTTRDLLRSQFK AAAQQLRDSLIYDVTVSMKLKAAEEATNKGDLAAAEKALAEAQDALTKATAFKADLTTKQ ATVKAAYEAKVAPAVVGVSAVNSRTVQIKFNKPIDASTVLVDKGTTDTSDDTLKTTSIVF TALDGQPAISQTDIKASLSDDKKTLTLVAANSDFFTKRYVVDIKNVKTTDGKDVPAYTTT IDTTDSVRPAVLSYSYADNGLTLKVKFSEPLNSVGTVKLYDGTTEISVSPSFTAGSDEMT INLASSSVPVNKALTLKIFGAVDYNGNVINPNPAELTVMKTTVDTTKPTVQSVEAVNDKT VKVTFSEKLLGNPTIKIGGTTAASVSVDSTGLVYTATLNSAQLGIQAVEVSSYTDLAGNV GDAYTKVVELKADTTAPKLVSSQVVKINGIENLVLTFDEEVTTQNNITVVSSNDYYVDEN NVRKQVGVTLTTNSTNFKLYNPVNGKSKSVALDISSLPKGTYTVTLPTGATALVKDLASN PNAYAEGKQITFVRGTDSLTTKPALDTNVSTNGVEVVDNNTLRFTFTQNLDASALNLSNF NINGVALSKAVFDGATNKILVTLAPGANTWTGTHVITVSNIKNVSGIAMDTVTTTESMNE NVAPTFTATLTS*(792)ADVIKVTFSEPVAHSTLSNAITGNNFTVKVDGTLNNVTGVYTDSAATT PVSATGNTGYKTVYLKLATPVTDLTKPITVSATNLVDVSAEGASPTVVGNTVSSDVVNVA K |
| Sequence Around Glycosites (21 AA) | VAPTFTATLTSADVIKVTFSE |
| Technique(s) used for Glycosylation Detection | Periodic acid-Schiff (PAS) staining and chemical deglycosylation |
| Technique(s) used for Glycosylated Residue(s) Detection | ESI-QTOF-MS (electrospray ionization quadrupole-time-of-flight mass spectrometry) |
| Glycan Information | |
| Glycan Annotation | Linkage:β-D-Gal-Ser/Thr. [→2)-α-L-Rhap-(1→3)-α-D-Fucp-(1→]n=~20. Rhamnose residue at the nonreducing end of the terminal repeating unit of the glycan chain is di-substituted. (R)-N-acetylmuramic acid found in an α-linkage to carbon 3 of the terminal rhamnose residue, serving as capping motif of an S-layer glycan. In addition, that rhamnose is substituted at position 2 with aβ-N-acetylglucosamine residue. The S-layer glycan chains are bound via the trisaccharide core →2)-α-L-Rhap-(1→3)-α-L-Rhap-(1→3)-α-L-Rhap-(1→ to carbon 3 ofβ-D-galactose, which is attached to S and T residues. |
| BCSDB ID | 23139 |
| GlyTouCan | G10237KB |
| Technique(s) used for Glycan Identification | HPAEC/PAD (high performance anion-exchange chromatography/pulsed amperometric detection), 1H and 13C NMR spectroscopy including 2D NOESY (nuclear Overhauser enhancement spectroscopy), HMBC (heteronuclear multiple bond correlation spectroscopy) and TOCSY (total correlation spectroscopy) |
| Literature | |
| Year of Identification | 2005 |
| Year of Identification Month Wise | 2005.4.27 |
| Year of Validation | 2007 |
| Reference | Messner, P., Steiner, K., Zarschler, K. and Schäffer, C., 2008. S-layer nanoglycobiology of bacteria. Carbohydrate Research, 343(12), pp.1934-1951. |
| Corresponding Author | Christina Schaffer Paul Messner |
| Contact | Center for NanoBiotechnology, University of Natural Resources and Applied Life Sciences Vienna, A-1190 Vienna, Austria |
| Reference | Zayni, S., Steiner, K., Pföstl, A., Hofinger, A., Kosma, P., Schäffer, C. and Messner, P., 2007. The dTDP-4-dehydro-6-deoxyglucose reductase encoding fcd gene is part of the surface layer glycoprotein glycosylation gene cluster of Geobacillus tepidamans GS5-97T. Glycobiology, 17(4), pp.433-443. |
| Corresponding Author | Paul Messner |
| Contact | University of Natural Resources and Life Sciences, Vienna, Center for NanoBiotechnology A-1180 Vienna, Gregor-Mendel-Strasse 33, Austria. |
| Reference | Kählig, H., Kolarich, D., Zayni, S., Scheberl, A., Kosma, P., Schäffer, C. and Messner, P., 2005. N-acetylmuramic acid as capping element of α-d-fucose-containing S-layer glycoprotein glycans from Geobacillus tepidamans GS5–97T. Journal of Biological Chemistry, 280(21), pp.20292-20299. |
| Corresponding Author | Christina Schaffer |
| Contact | University of Natural Resources and Life Sciences, Vienna, Center for NanoBiotechnology A-1180 Vienna, Gregor-Mendel-Strasse 33, Austria. |