ProGT87 (HMW1CAa)
| ProGT ID | ProGT87 (HMW1CAa) |
| Organism Information | |
| Organism Name | Aggregatibacter aphrophilus strain NJ8700 |
| Clinical Implication | Pathogenic |
| Domain | Bacteria |
| Classification | Phylum : Proteobacteria Class : GammaProteobacteria Orders : Pasteurellales Family : Pasteurellaceae Genus : Aggregatibacter Species : aphrophilus Strain : NJ8700 |
| Taxonomic ID (NCBI) | 634176 |
| Genome Information | |
| Gene Bank | NC_012913 |
| Gene Information | |
| Gene Name | hmw1CAa |
| NCBI Reference Sequence | ALC78880.1 |
| Protein information | |
| Protein Name | HMW1CAa |
| UniProtKB/ SwissProt ID | A0A0M5J8N3 |
| UniProtKB Sequence | >tr|A0A0M5J8N3|A0A0M5J8N3_AGGAP Hmw1C OS=Aggregatibacter aphrophilus GN=hmw1C PE=4 SV=1 MSRKKNPSVIQFEKAITEKNYEAACTELLDILNKIDTNFGDIEGIDFDYPQQLETLMQDR IVYFCTRMSNAITQLFCDPQFSLSESGANRFFVVQRWLNLIFASSPYINADHILQTYNCN PERDSIYDIYLEPNKNVLMXFAVLYLPESNVNLNLDTMWETDKNICGSLCFALQSPRFIG TPAAFSKRSTILQWFPAKLEQFHVLDDLPSNISHDVYMHCSYDTAENKHNVKKALNQVIR SHLLKCGWQDRQITQIGMRNGKPVMVVVLEHFHSSHSIYRTHSTSMIAAREQFYLIGLGN NAVDQAGRDVFDEFHEFDGSNILKKLAFLKEMCEKNDAAVLYMPSIGMDLATIFVSNARF APIQVIALGHPATTHSEFIEYVIVEDDYVGSESCFSETLLRLPKDALPYVPSSLAPTDVQ YVLRETPEVVNIGIAATTMKLNPYFLETLKTIRDRAKVKVHFHFALGQSIGITHPYVARF IRSYLGDDATAHPHSPYNRYLDILHNCDMMLNPFPFGNTNGIIDMVTLGLVGVCKTGPEV HEHIDEGLFKRLGLPEWLIADSVEDYIERAIRLAENHQERLALRRHIIENNGLKTLFSGD PSPMGKTLFAKLTEWRQTNGI |
| EMBL CDS | ALC78880.1 |
| Sequence length | 621 AA |
| Subcellular Location | Cytoplasm |
| Function in Native Organism | 1) Glycosylation is important for autoaggregation and adherence to human epithelial cells. |
| Potential Application | 1) Designing novel inhibitors against HMW1C-like enzyme may have therapeutic potential. 2) Glycoprotein EmaA may be the potential candidate for vaccines production. |
| Additional Information | 1) HMW1CAa encode an HMW1C-like enzyme that glycosylates an autotransporter protein EmaA. 2) First examples of trimeric autotransporters that are modified by HMW1C-like enzymes. |
| Glycosyltransferase Information | |
| Glycosylation Type | N- (Asn) linked |
| CAZY Family | GT41 |
| EC Number (BRENDA) | 2.4.99.18 |
| Mechanism of Glycan Transfer | Sequential |
| Acceptor specificity Sequon_1 | Asn-Xaa-Ser/Thr |
| Donor Type | UDP-Hexose |
| Donor Specificity | Nucleotide activated sugars |
| Glycan Information | |
| Glycan transferred | Monosaccharide (Hexose) |
| Method of Glycan Indentification | LC-MS/MS |
| Experimental_strategies | In vivo and In vitro |
| Acceptor Subtrate Information | |
| Acceptor Substrate name | EmaA |
| ProGPdb ID | ProGP514 |
| Litrature | |
| Year Of Validation | 2015 |
| Reference | Rempe, K.A., Spruce, L.A., Porsch, E.A., Seeholzer, S.H., Nørskov-Lauritsen, N. and St. Geme III, J.W., 2015. Unconventional N-linked glycosylation promotes trimeric autotransporter function in Kingella kingae and Aggregatibacter aphrophilus. MBio, 6(4), pp.e01206-15. |
| Corresponding Author | The Children's Hospital of Philadelphia, Philadelphia, Pennsylvania, USA University of Pennsylvania Perelman School of Medicine, Philadelphia, Pennsylvania, USA |