Latest update: September 24, 2018


ProGT87 (HMW1CAa)

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ProGT ID ProGT87 (HMW1CAa)
Organism Information
Organism NameAggregatibacter aphrophilus strain NJ8700
Clinical ImplicationPathogenic
DomainBacteria
PhylumProteobacteria
ClassificationFamily: Pasteurellaceae
Order: Pasteurellales
Class: Gammaproteobacteria
Phylum: Proteobacteria
Taxonomic ID (NCBI)732
Genome Information
Gene BankNC_012913
Gene Information
Gene Namehmw1CAa
NCBI Reference SequenceALC78880.1
Protein information
Protein NameHMW1CAa 
UniProtKB/ SwissProt IDA0A0M5J8N3
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 CDSALC78880.1
Sequence length621 AA
Subcellular LocationCytoplasm
Function in Native Organism 1) Glycosylation is important for autoaggregation and adherence to human epithelial cells.
Potential Application1) Designing novel inhibitors against HMW1C-like enzyme may have therapeutic potential.
2) Glycoprotein EmaA may be the potential candidate for vaccines production.
Additional Information1) 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 TypeN- (Asn) linked 
CAZY FamilyGT41
EC Number (BRENDA)2.4.99.18
Mechanism of Glycan TransferSequential
Acceptor specificity Sequon_1Asn-Xaa-Ser/Thr
Donor TypeNucleotide activated sugars
Donor SpecificityUDP-Hexose
Glycan Information
Glycan transferredMonosaccharide (Hexose) 
Method of Glycan IndentificationLC-MS/MS
Experimental_strategiesIn vivo and In vitro 
Acceptor Subtrate Information
Acceptor Substrate name EmaA
ProGPdb ID ProGP514
Litrature
Year Of Validation2015 
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 groupsThe Childrens Hospital of Philadelphia, Philadelphia, Pennsylvania, USA University of Pennsylvania Perelman School of Medicine, Philadelphia, Pennsylvania, USA
Corresponding Author Geme, J. W. S.
ContactsThe Childrens Hospital of Philadelphia, Philadelphia, Pennsylvania, USA University of Pennsylvania Perelman School of Medicine, Philadelphia, Pennsylvania, USA