| ProGlyProt ID | BU107 |
| Organism Information |
| Organism Name | Aggregatibacter actinomycetemcomitans |
| Domain | Bacteria |
| Classification | Family: Pasteurellaceae
Order: Pasteurellales
Class: Gammaproteobacteria
Division or phylum: "Proteobacteria" |
| Taxonomic ID (NCBI) | |
| Genome Sequence (s) |
| GeneBank | |
| EMBL | |
| Gene Information |
| Gene Name | emaA |
| NCBI Gene ID | |
| Protein Information |
| Protein Name | Extracellular matrix protein adhesin A (EmaA) |
| UniProtKB/SwissProt ID | |
| NCBI RefSeq | |
| EMBL-CDS | |
| UniProtKB Sequence | |
| Sequence length | |
| Subcellular Location | Extracellular |
| Function | EmaA monomers trimerize to form antennae-like structures on the surface of the bacterium required for collagen binding. |
| Glycosylation Status |
| Glycosylation Type | Information currently not available with us. |
| Technique(s) used for Glycosylation Detection | Lectin binding. |
| Literatures |
| Reference(s) | 1) Tang, G. and Mintz, K.P. (2010) Glycosylation of the collagen adhesin EmaA of Aggregatibacter actinomycetemcomitans is dependent upon the lipopolysaccharide biosynthetic pathway. J Bacteriol, 192, 1395-1404. [PubMed: 20061477] |
| Year of Identification | 2010 |
