ProGT ID | ProGT37.1 (Gtf3) |
Organism Information | |
Organism Name | Streptococcus parasanguinis FW213 |
Domain | Bacteria |
Phylum | Firmicutes |
Classification | Family: Streptococcaceae Order: Lactobacillales Class: Bacilli (or Firmibacteria) Division or phylum: "Firmicutes" |
Taxonomic ID (NCBI) | 1318 |
Genome Information | |
Gene Bank | EU821531 |
EMBL | EU821531 |
Gene Information | |
Gene Name | nss |
NCBI Reference Sequence | ACF35267.1 |
Protein information | |
Protein Name | Gtf3Â |
UniProtKB/ SwissProt ID | B5A7L9 |
UniProtKB Sequence | >tr|B5A7L9|B5A7L9_STRPA Nucleotide sugar synthetase-like protein OS=Streptococcus parasanguinis GN=nss PE=1 SV=1 MRVYITNINGQSIQSTAQLCQNTVTDVAVSLGYRELGIYCYQIHTDSESELSKRLDGIVA GLRHGDVVIFQTPTWNTTEFDEKLMNKLKLYDIKIVLFIHDVVPLMFSGNFYLMDRTIAY YNKADVVVAPSQKMIDKLRDFGMNVSKTVVQGMWDHPTQAPMFPAGLKREIHFPGNPERF SFVKEWKYDIPLKVYTWQNVELPQNVHKINYRPDEQLLMEMSQGGFGLVWMDDKDKEYQS LYCSYKLGSFLAAGIPVIVQEGIANQELIENNGLGWIVKDVEEAIMKVKNVNEDEYIELV KNVRSFNPILRKGFFTRRLLTESVFQAICD |
EMBL CDS | ACF35267.1. |
Sequence length | 330 AA |
PDB ID (Structural Information) | 3QKW, 3RHZ |
Glycosylation Information | |
CAZY Family | GTNC |
EC Number (BRENDA) | 2.4.1.- |
Sugar Donor Specificity | UDP-Glc |
Acceptor Substrate Specificity | Glc-GalNAc modified Fap1 |
Experimental Validation | In vitro and In vivo |
Donor Specificity | UDP-Glc |
Function in Glycosylation pathway | 1) Transfer Glucose to the Glc-GalNAc modified Fap1. |
Additional Information | 1) Gtf3 transfer Glucose on previously modified Fap1 protein and it also plays an important role in the biofilm formation by S. parasanguinis. |
Litrature | |
Year Of Validation | 2010Â |
Reference | Zhou, M., Zhu, F., Dong, S., Pritchard, D., & Wu, H. (2010). A novel glucosyltransferase is required for glycosylation of a serine-rich adhesin and biofilm formation by Streptococcus parasanguinis. Journal of Biological Chemistry, jbc-M109. |
Authors | Zhou, M., Zhu, F., Dong, S., Pritchard, D., & Wu, H. |
Research groups | Department of Pediatric Dentistry, University of Alabama at Birmingham, Birmingham, Alabama 35244, USA |
Corresponding Author | Wu, H. |
Contacts | Department of Pediatric Dentistry, University of Alabama at Birmingham, Birmingham, Alabama 35244, USA |
Reference | Zhu, F., Erlandsen, H., Ding, L., Li, J., Huang, Y., Zhou, M., ... & Wu, H. (2011). Structural and functional analysis of a new subfamily of glycosyltransferases required for glycosylation of serine-rich streptococcal adhesins. Journal of Biological Chemistry, jbc-M110. |
Authors | Zhu, F., Erlandsen, H., Ding, L., Li, J., Huang, Y., Zhou, M., ... & Wu, H. |
Research groups | Department of Pediatric Dentistry and Microbiology, University of Alabama at Birmingham, Schools of Dentistry and Medicine, Birmingham, Alabama 35294, USA |
Corresponding Author | Wu, H. |
Contacts | Department of Pediatric Dentistry and Microbiology, University of Alabama at Birmingham, Schools of Dentistry and Medicine, Birmingham, Alabama 35294, USA |
Reference | Zhu, F., Zhang, H., Yang, T., Haslam, S. M., Dell, A., & Wu, H. (2016). Engineering and dissecting the glycosylation pathway of a streptococcal serine-rich repeat adhesin. Journal of Biological Chemistry, jbc-M116. |
Authors | Zhu, F., Zhang, H., Yang, T., Haslam, S. M., Dell, A., & Wu, H. |
Research groups | 1 University of Alabama at Birmingham, United States.
2 Imperial College London, United Kingdom.
3 University of Alabama at Birmingham, United States |
Corresponding Author | Wu, H. |
Contacts | University of Alabama at Birmingham, United States |