ProGT88 (HMW1CKk)
| ProGT ID | ProGT88 (HMW1CKk) |
| Organism Information | |
| Organism Name | Kingella kingae strain 269-492 |
| Clinical Implication | Pathogenic |
| Domain | Bacteria |
| Phylum | Proteobacteria |
| Classification | Family: Neisseriaceae Order: Neisseriales Class: Betaproteobacteria Division or phylum: "Proteobacteria" |
| Taxonomic ID (NCBI) | 504 |
| Genome Information | |
| Gene Bank | LN869922 |
| EMBL | LN869922 |
| Gene Information | |
| Gene Name | hmw1CKk |
| NCBI Gene ID | 29365636 |
| NCBI Reference Sequence | CRZ19328.1 |
| Protein information | |
| Protein Name | HMW1CKk |
| UniProtKB/ SwissProt ID | A0A0P1CZQ3 |
| UniProtKB Sequence | >tr|A0A0P1CZQ3|A0A0P1CZQ3_9NEIS Adhesin processing protein OS=Kingella kingae GN=KKKWG1_0152 PE=4 SV=1 MTQTTEQSIPSLTRFEQAVSSQNYEAACTELLSILGQLDSNFGEIHGIEFAYPVQLQNLQ QDVTIHFCTRMATAITTLFTNKMWSLTDDGRTRFLTVQRWINMIFASSPYVNADHVLATY NTNPEPDSLWNNIHLDNNQSAFNKFAVMYLPESNVQVNLDSLWSVNPSLTASLCFAWQSP RFIATEAAFNRRAQVLQWFPAKLAQFNNLNTLPANISHDVYMHCSYDIEPNKHDVKGALN QVIRRHILEEYGWQDCDVTKIGNAHGKPVMLVLLEHFHSGHSIYRTHSTSMIAAREQFYL IGIGGAAVDEAGRAVFDEFVEIDAKASTMEKLQAIRAIATKEQPAVFYMPSIGMDLITIF ASNTRIAPIQVIALGHPATTHSKFIEYVIVEDDYVGSEECFSETLLRLPKDALPYVPSAL APASVEYNLRENPSVVHIGVASTTMKLNPYFLRACAEIKARSKVPVHFHFAMGQASGVTF AYIERFLKTYLGKAVTAYPHQSYTDYLRTLHQCDMMINPFPFGNTNGIIDMVTLGLVGIC KTGAEVHEHIDEGLFKRLGLPEWLITQTADDYVNCAVRLAENHEERLALRRHIIENNGLN TLFSGDPKPMGQILWAKVQEKMAKPAKKATAKVASKPATAVEPVAEKPATKTVRKTASKK AAATEATTEKAAPKTTRTRKKAAE |
| EMBL CDS | CRZ19328.1 |
| Sequence length | 684 AA |
| Subcellular Location | Cytoplasm |
| Function in Native Organism | 1) Glycosylation is important for autoaggregation and adherence to human epithelial cells. |
| Potential Application | 1) Glycoprotein Knh may be the potential candidate for vaccines production. 2) The first step in infection is adherence to host tissue, the ability to interrupt HMW1C-mediated glycosylation may have therapeutic potential. |
| Additional Information | 1) First examples of trimeric autotransporters that are modified by HMW1C-like enzymes. 2) Glycosylation required for normal functioning such as adherence and autoaggregation of acceptor protein. |
| Glycosyltransferase Information | |
| Glycosylation Type | N- (Asn) linked |
| CAZY Family | GT41 |
| EC Number (BRENDA) | 2.4.1.- |
| 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) |
| Method of Glycan Indentification | LC-MS/MS |
| Experimental_strategies | In vivo and In vitro |
| Acceptor Subtrate Information | |
| Acceptor Substrate name | Knh |
| ProGPdb ID | ProGP513 |
| Litrature | |
| Year Of Validation | 2015 |
| 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 |