ProGT87 (HMW1CAa)
ProGT ID | ProGT87 (HMW1CAa) |
Organism Information | |
Organism Name | Aggregatibacter aphrophilus strain NJ8700 |
Clinical Implication | Pathogenic |
Domain | Bacteria |
Phylum | Proteobacteria |
Classification | Family: Pasteurellaceae Order: Pasteurellales Class: Gammaproteobacteria Phylum: Proteobacteria |
Taxonomic ID (NCBI) | 732 |
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 | Nucleotide activated sugars |
Donor Specificity | UDP-Hexose |
Glycan Information | |
Glycan transferred | Monosaccharide (Hexose)Â |
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 | 2015Â |
Reference | Rempe, K. A., Spruce, L. A., Porsch, E. A., Seeholzer, S. H., Nørskov-Lauritsen, N., & Geme, J. W. S. (2015). Unconventional N-linked glycosylation promotes trimeric autotransporter function in kingella kingae and Aggregatibacter aphrophilus. MBio, 6(4), e01206-15. |
Authors | Rempe, K. A., Spruce, L. A., Porsch, E. A., Seeholzer, S. H., Nørskov-Lauritsen, N., & Geme, J. W. S. |
Research groups | The Childrens Hospital of Philadelphia, Philadelphia, Pennsylvania, USA University of Pennsylvania Perelman School of Medicine, Philadelphia, Pennsylvania, USA |
Corresponding Author | Geme, J. W. S. |
Contacts | The Childrens Hospital of Philadelphia, Philadelphia, Pennsylvania, USA University of Pennsylvania Perelman School of Medicine, Philadelphia, Pennsylvania, USA |