| IED ID | IndEnz0002015693 |
| Enzyme Type ID | protease015693 |
| Protein Name |
UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase GtfA subunit EC 2.4.1.- Glycosyltransferase Gtf1 Glycosyltransferase GtfA |
| Gene Name | gtfA gtf1 |
| Organism | Streptococcus parasanguinis |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Lactobacillales Streptococcaceae Streptococcus Streptococcus parasanguinis |
| Enzyme Sequence | MTIYNINLGIGWASSGVEYAQAYRAQILRSLGMPAKFIFTNMFQSENLEHFTKNIGFEDNEIIWLYGYFTDVKISGTTYKKDDLEATFSQCPTKKEASSDRKLIRYYFENQELYINASLYGENQEYVQRVEYVVKGKLIRKDYYSYTKVFSEFYSPGENGVQLCNRSFYNEDGSIAYEEILSNEKSTFVFSNKICYGLEELLEFMLEDLSLTKSDLILLDRATGIGQVVFENIGAAKLAVVIHAEHFNEKNTDEHNILWNNYYEYQFTNADKVNAFITSTERQKILLEEQFTQYTSLHPKIVAIPVGSLDQLKFPEQSRKSFSMMTGSRLAIEKHIDWLIEGVALAQKRLPELTFDIYGEGGERRKLTELLTKLHAGEFIELKGHKQLDEIYQNYELYLTASTSEGFGLTLMEAVGSGLPIIGFDVPYGNQTFVCSGENGLLIERPKGDDRSRIVQAFADSIYEYFTKFKMADAQQYSYNIAENYKHEKLVERWKDFIEEMLND |
| Enzyme Length | 504 |
| Uniprot Accession Number | A1C3L9 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 243; /note=N-acetyl-D-glucosamine; /evidence=ECO:0000255|HAMAP-Rule:MF_01472 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-[N-acetyl-alpha-D-glucosaminyl]-L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:59872, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:15471, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:143279; Evidence={ECO:0000255|HAMAP-Rule:MF_01472}; |
| DNA Binding | |
| EC Number | 2.4.1.- |
| Enzyme Function | FUNCTION: Required for polymorphic O-glycosylation of serine-rich repeat protein Fap1. Catalyzes the first step in glycosylation by transferring N-acetylglucosamine from UDP-GlcNAc to serine residues in Fap1. Part of the accessory SecA2/SecY2 system specifically required to export Fap1, a serine-rich fimbrial adhesin encoded upstream in the same operon. The GtfA-GtfB (Gtf1-Gtf2 in this bacteria) complex adds GlcNAc from UDP-GlcNAc to Fap1, attaching the first sugar residue. Cannot use not UDP-Glc as substrate. This subunit has very low glycosyltransferase activity; the GtfB stabilizing protein enhances membrane association, protease resistance and glycosyltransferase activity. {ECO:0000269|PubMed:16997950, ECO:0000269|PubMed:18083807, ECO:0000269|PubMed:20971868}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Protein modification; protein glycosylation. {ECO:0000255|HAMAP-Rule:MF_01472}. |
| nucleotide Binding | NP_BIND 16..19; /note=UDP; /evidence=ECO:0000255|HAMAP-Rule:MF_01472; NP_BIND 385..386; /note=UDP; /evidence=ECO:0000255|HAMAP-Rule:MF_01472 |
| Features | Binding site (1); Chain (1); Nucleotide binding (2); Region (1) |
| Keywords | Cell membrane;Cytoplasm;Direct protein sequencing;Glycosyltransferase;Membrane;Nucleotide-binding;Transferase |
| Interact With | A1C3M0 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01472, ECO:0000269|PubMed:21862581}. Cell membrane {ECO:0000255|HAMAP-Rule:MF_01472, ECO:0000269|PubMed:21862581}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01472, ECO:0000305|PubMed:21862581}. Note=Cell membrane association requires GtfB (Gtf2), protein is more active and protected from trypsin (PubMed:21862581). {ECO:0000255|HAMAP-Rule:MF_01472, ECO:0000269|PubMed:21862581}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 58,239 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:59872 |
| Cross Reference Brenda |