Tag | Content |
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CPLM ID | CPLM-005562 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Lipopolysaccharide 1,2-N-acetylglucosaminetransferase |
Protein Synonyms/Alias | |
Gene Name | waaU |
Gene Synonyms/Alias | rfaK; waaK; b3623; JW3598 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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16 | KKRFYINKIKINFLS | acetylation | [1] | 151 | LGFDHWYKRYYSFYH | acetylation | [1] | 177 | TRAIEILKHIYGEGK | acetylation | [1] | 184 | KHIYGEGKFSTNYDL | acetylation | [1] | 200 | LPVDVEDKIKEFIGD | acetylation | [1] | 230 | RLTFEQIKVIYQEVK | acetylation | [1] | 325 | IWSPNHHKSIQIVSP | acetylation | [1] | 337 | VSPTYTVKDIDTETL | acetylation | [1] | 349 | ETLTNSVKRLSCIDK | acetylation | [1] |
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Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | Adds the terminal N-acetyl-D-glucosamine group on the glucose(II) group of LPS. |
Sequence Annotation | |
Keyword | Complete proteome; Glycosyltransferase; Lipopolysaccharide biosynthesis; Membrane; Reference proteome; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 357 AA |
Protein Sequence | MRLGTFHKKK RFYINKIKIN FLSFLFRNKI NNQITDPAQV KSCLIIHDNN KLGDLIVLSS 60 IYRELYSKGV KITLLTNRKG GEFLSNNKNI FEFCIKESTG FLEMLTLCKH LRDLQFDIVL 120 DPFETMPSFK HSLILSSLKD SYILGFDHWY KRYYSFYHPH DECLKEHMST RAIEILKHIY 180 GEGKFSTNYD LHLPVDVEDK IKEFIGDTRI VIINPLGAKK ICRLTFEQIK VIYQEVKTHF 240 ENYRIIFTGL PQDLLTIPIL EIETLPFDEF IYTVALTKYS DFVISVDTAL VHIAAAYHKP 300 TLAFYPNSRT PEYPSHLIWS PNHHKSIQIV SPTYTVKDID TETLTNSVKR LSCIDKK 357 |
Gene Ontology | GO:0016020; C:membrane; IEA:UniProtKB-SubCell. GO:0008917; F:lipopolysaccharide N-acetylglucosaminyltransferase activity; IEA:EC. GO:0009244; P:lipopolysaccharide core region biosynthetic process; IEA:UniProtKB-UniPathway. |
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