| Tag | Content |
|---|
| CPLM ID | CPLM-005556 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Lipopolysaccharide 1,2-glucosyltransferase |
Protein Synonyms/Alias | |
Gene Name | rfaJ |
Gene Synonyms/Alias | waaJ; b3626; JW3601 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 77 | GFFQKIAKLAEQNQL | acetylation | [1] | | 164 | DVEPMQEKAVSRLSD | acetylation | [1] | | 212 | MSKDNVYKYPDQDVM | acetylation | [1] | | 241 | YNTIYTIKSELKDKT | acetylation | [1] | | 245 | YTIKSELKDKTHQNY | acetylation | [1] | | 282 | WAIYPSVKYYKIALE | acetylation | [1] | | 308 | AKSIIEFKKRYKHLL | acetylation | [1] |
|
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 | |
Sequence Annotation | |
Keyword | Complete proteome; Glycosyltransferase; Lipopolysaccharide biosynthesis; Reference proteome; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 338 AA |
Protein Sequence | MDSFPAIEID KVKAWDFRLA NINTSECLNV AYGVDANYLD GVGVSITSIV LNNRHINLDF 60
YIIADVYNDG FFQKIAKLAE QNQLRITLYR INTDKLQCLP CTQVWSRAMY FRLFAFQLLG 120
LTLDRLLYLD ADVVCKGDIS QLLHLGLNGA VAAVVKDVEP MQEKAVSRLS DPELLGQYFN 180
SGVVYLDLKK WADAKLTEKA LSILMSKDNV YKYPDQDVMN VLLKGMTLFL PREYNTIYTI 240
KSELKDKTHQ NYKKLITEST LLIHYTGATK PWHKWAIYPS VKYYKIALEN SPWKDDSPRD 300
AKSIIEFKKR YKHLLVQHHY ISGIIAGVCY LCRKYYRK 338 |
Gene Ontology | GO:0008918; F:lipopolysaccharide 3-alpha-galactosyltransferase activity; IEA:InterPro. GO:0008919; F:lipopolysaccharide glucosyltransferase I activity; IEA:EC. GO:0009244; P:lipopolysaccharide core region biosynthetic process; IEA:UniProtKB-UniPathway. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |