ProGT67 (SdgB)
| ProGT ID | ProGT67 (SdgB) |
| Organism Information | |
| Organism Name | Staphylococcus aureus |
| Clinical Implication | Pathogenic |
| Domain | Bacteria |
| Classification | Phylum : Firmicutes Class : Bacilli Orders : Bacillales Family : Staphylococcaceae Genus : Staphylococcus Species : aureus Strain : USA300 |
| Taxonomic ID (NCBI) | 367830 |
| Genome Information | |
| Gene Bank | CP000255.1 |
| EMBL | CP000255 |
| Gene Information | |
| Gene Name | SAUSA300_0550 |
| NCBI Reference Sequence | ABD21647.1 |
| Protein information | |
| Protein Name | SdgB |
| UniProtKB/ SwissProt ID | A0A0H2XGN0 |
| NCBI Ref Seq | WP_001106113.1 |
| UniProtKB Sequence | >tr|A0A0H2XGN0|A0A0H2XGN0_STAA3 Glycosyl transferase, group 1 family protein OS=Staphylococcus aureus (strain USA300) GN=SAUSA300_0550 PE=4 SV=1 MNYFVGNSLGVNLTGIEKAIINRLNLFKEMGRPAQCVFLSWNRYLYRNAQNYITSSDYIN MYDFFQEATYLERNEPFDWLSYWTDECHYTLKHVENSHDFRIYDQERFLMYAHFQDPKYR ILDYVNHFDSQRRKVKRDFYDVRGFLSCSRILVDKQQTLCEFFYNPEGDTKLEKYFSYKD GKPEVQKIIVYYANKQYFFNNETELGAFFIKQLYQHGDLFFSDRNVYTAPIFNLTPESIP VVAVLHSTHIKNIDALDSSPFKNVYKAMFENLSRYRAIIVSTEQQKLDVEKRINHTIPVV NIPVGYSETIDTPVQTLDQRSVKLISVARYSPEKQLHQQIELIKRLVSYVPKIELHMYGF GSESKKLNELIQKYGLENHVYLRGFLSNLDQEYSDAYLSLITSNMEGFSLALLESLAHGV PVISYDIKYGPNELITSDFNGYLITKNDEDALFDKVKYVIDHPEVQQRLSKGSLAKAQQY SKASLIKQWDQFVRLI |
| EMBL CDS | ABD21647.1 |
| Sequence length | 496 AA |
| Function in Native Organism | 1) SdgB transfer the first GlcNAc to the SDR Protein. |
| Potential Application | |
| Additional Information | 1) SdgB adds GlcNAc residue to the SDR protein. 2) SdgB creates an immunodominant epitope for highly opsonic human antibodies by transferring GlcNAc residue on SDR-proteins. 3) aggB (sdgA) and aggC (sdgB) are involved in GlcNAc modification of the ClfA SD repeats. |
| Glycosyltransferase Information | |
| Glycosylation Type | O- (Ser/Thr) linked |
| CAZY Family | GT4 |
| EC Number (BRENDA) | 2.4.1.109 |
| Mechanism of Glycan Transfer | Sequential |
| Acceptor specificity Sequon_1 | Serine-Aspartate dipeptide-Repeats (SDR) |
| Donor Type | UDP-GlcNAc |
| Donor Specificity | Nucleotide activated sugars |
| Glycan Information | |
| Glycan transferred | Monosaccharide (GlcNAc) |
| Method of Glycan Indentification | LC-MS |
| Experimental_strategies | In vivo and In vitro |
| Acceptor Subtrate Information | |
| Acceptor Substrate name | Pls (Plasmin sensitive surface protein) |
| ProGPdb ID | ProGP551 |
| Acceptor Substrate name | ClfASD5 |
| Litrature | |
| Year Of Validation | 2013 |
| Reference | Hazenbos, W.L., Kajihara, K.K., Vandlen, R., Morisaki, J.H., Lehar, S.M., Kwakkenbos, M.J., Beaumont, T., Bakker, A.Q., Phung, Q., Swem, L.R. and Ramakrishnan, S., 2013. Novel staphylococcal glycosyltransferases SdgA and SdgB mediate immunogenicity and protection of virulence-associated cell wall proteins. PLoS pathogens, 9(10), p.e1003653. |
| Corresponding Author | Dept. of Infectious Diseases, Genentech, Inc., San Francisco, California, United States of America |
| Reference | Thomer, L., Becker, S., Emolo, C., Quach, A., Kim, H.K., Rauch, S., Anderson, M., LeBlanc, J.F., Schneewind, O., Faull, K.F. and Missiakas, D., 2014. N-acetylglucosaminylation of serine-aspartate repeat proteins promotes Staphylococcus aureus bloodstream infection. Journal of Biological Chemistry, 289(6), pp.3478-3486. |
| Corresponding Author | Department of Microbiology, The University of Chicago, Chicago, Illinois 60637 |
| Reference | Kim, D.G., Baek, I., Lee, Y., Kim, H., Kim, J.Y., Bang, G., Kim, S., Yoon, H.J., Han, B.W., Suh, S.W. and Kim, H.S., 2021. Structural basis for SdgB-and SdgA-mediated glycosylation of staphylococcal adhesive proteins. Acta Crystallographica Section D: Structural Biology, 77(11). |
| Corresponding Author | Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul 08826, Republic of Korea Department of Chemistry, College of Natural Sciences, Seoul National University, Seoul 08826, Republic of Korea Research Institute, National Cancer Center, Goyang, Gyeonggi 10408, Republic of Korea |