| Organism Information |
| Organism Name | Streptococcus parasanguinis |
| Clinical Implication | Pathogenic |
| 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 | DQ990875 |
| EMBL | DQ990875 |
| Gene Information |
| Gene Name | gtf1 |
| Protein information |
| Protein Name | Gtf1 |
| UniProtKB/ SwissProt ID | A1C3L9 |
| NCBI Ref Seq | WP_014713989.1. |
| UniProtKB Sequence | >sp|A1C3L9|GTF1_STRPA Glycosyltransferase Gtf1 OS=Streptococcus parasanguinis GN=gtf1 PE=1 SV=1
MTIYNINLGIGWASSGVEYAQAYRAQILRSLGMPAKFIFTNMFQSENLEHFTKNIGFEDN
EIIWLYGYFTDVKISGTTYKKDDLEATFSQCPTKKEASSDRKLIRYYFENQELYINASLY
GENQEYVQRVEYVVKGKLIRKDYYSYTKVFSEFYSPGENGVQLCNRSFYNEDGSIAYEEI
LSNEKSTFVFSNKICYGLEELLEFMLEDLSLTKSDLILLDRATGIGQVVFENIGAAKLAV
VIHAEHFNEKNTDEHNILWNNYYEYQFTNADKVNAFITSTERQKILLEEQFTQYTSLHPK
IVAIPVGSLDQLKFPEQSRKSFSMMTGSRLAIEKHIDWLIEGVALAQKRLPELTFDIYGE
GGERRKLTELLTKLHAGEFIELKGHKQLDEIYQNYELYLTASTSEGFGLTLMEAVGSGLP
IIGFDVPYGNQTFVCSGENGLLIERPKGDDRSRIVQAFADSIYEYFTKFKMADAQQYSYN
IAENYKHEKLVERWKDFIEEMLND
|
| EMBL CDS | ABL74004.1 |
| Sequence length | 504 AA |
| Subcellular Location | Membrane (Integral component of membrane) |
| Function in Native Organism | 1) The complex of two GTs namely Gtf1 and Gtf2 initiates the glycosylation of by transferring the GlcNAc to Fap 1 protein. |
| Potential Application | 1) Studying biosynthetic pathways and the enzymes involved in biofilm formation may help to design of new potential therapeutics to control bacterial biofilm formation in future. |
| Additional Information | 1) The N-terminal domain of Gtf1 directly interacts with Gtf2 and this interaction plays a critical role in Fap1 glycosylation. |
| Glycosyltransferase Information |
| Glycosylation Type | O- (Ser/Thr) linked |
| CAZY Family | GT4 |
| EC Number (BRENDA) | 2.4.1.- |
| Mechanism of Glycan Transfer | Sequential |
| Donor Type | Nucleotide activated sugars |
| Donor Specificity | UDP-GlcNAc |
| Accessory GT ID | ProGT37.1ProGT37.2 |
| Glycan Information |
| Glycan transferred | Monosaccharide (GlcNAc) |
| Method of Glycan Indentification | GC-MS |
| Experimental_strategies | In vitro and In vivo |
| Acceptor Subtrate Information |
| Acceptor Substrate name | Fap1 |
| ProGPdb ID | ProGP209 |
| Litrature |
| Year Of Validation | 2010 |
| 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., 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 | University of Alabama at Birmingham, United States
|
| Corresponding Author | Wu, H.
|
| Contacts | University of Alabama at Birmingham, United States
|
| Reference | Zhang, H., Zhou, M., Yang, T., Haslam, S. M., Dell, A., & Wu, H. (2016). A new helical binding domain mediates a unique glycosyltransferase activity of a bifunctional protein. Journal of Biological Chemistry, jbc-M116.
|
| Authors | Zhang, H., Zhou, M., Yang, T., Haslam, S. M., Dell, A., & Wu, H.
|
| Research groups | University of Alabama at Birmingham, United States
|
| Corresponding Author | Wu, H.
|
| Contacts | University of Alabama at Birmingham, United States
|
