Tag | Content |
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CPLM ID | CPLM-002687 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Chaperone protein DnaJ |
Protein Synonyms/Alias | HSP40; Heat shock protein J |
Gene Name | dnaJ |
Gene Synonyms/Alias | groP; b0015; JW0014 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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31 | AYKRLAMKYHPDRNQ | acetylation | [1] | 41 | PDRNQGDKEAEAKFK | acetylation | [1] | 46 | GDKEAEAKFKEIKEA | acetylation | [1] | 51 | EAKFKEIKEAYEVLT | acetylation | [1] | 62 | EVLTDSQKRAAYDQY | acetylation | [1] | 194 | QGRGTLIKDPCNKCH | acetylation | [2] | 215 | RSKTLSVKIPAGVDT | acetylation | [1] | 292 | LDGRVKLKVPGETQT | acetylation | [1] | 301 | PGETQTGKLFRMRGK | acetylation | [1] | 361 | EHNSPRSKSFFDGVK | acetylation | [1] | 368 | KSFFDGVKKFFDDLT | acetylation | [1] | 369 | SFFDGVKKFFDDLTR | 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] [2] Comprehensive profiling of protein lysine acetylation in Escherichia coli. Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z. J Proteome Res. 2013 Feb 1;12(2):844-51. [ PMID: 23294111] |
Functional Description | Interacts with DnaK and GrpE to disassemble a protein complex at the origins of replication of phage lambda and several plasmids. Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. |
Sequence Annotation | DOMAIN 3 72 J. REPEAT 144 151 CXXCXGXG motif. REPEAT 161 168 CXXCXGXG motif. REPEAT 183 190 CXXCXGXG motif. REPEAT 197 204 CXXCXGXG motif. ZN_FING 131 209 CR-type. METAL 144 144 Zinc 1. METAL 147 147 Zinc 1. METAL 161 161 Zinc 2. METAL 164 164 Zinc 2. METAL 183 183 Zinc 2. METAL 186 186 Zinc 2. METAL 197 197 Zinc 1. METAL 200 200 Zinc 1. |
Keyword | 3D-structure; Chaperone; Complete proteome; Cytoplasm; Direct protein sequencing; DNA replication; Metal-binding; Reference proteome; Repeat; Stress response; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 376 AA |
Protein Sequence | MAKQDYYEIL GVSKTAEERE IRKAYKRLAM KYHPDRNQGD KEAEAKFKEI KEAYEVLTDS 60 QKRAAYDQYG HAAFEQGGMG GGGFGGGADF SDIFGDVFGD IFGGGRGRQR AARGADLRYN 120 MELTLEEAVR GVTKEIRIPT LEECDVCHGS GAKPGTQPQT CPTCHGSGQV QMRQGFFAVQ 180 QTCPHCQGRG TLIKDPCNKC HGHGRVERSK TLSVKIPAGV DTGDRIRLAG EGEAGEHGAP 240 AGDLYVQVQV KQHPIFEREG NNLYCEVPIN FAMAALGGEI EVPTLDGRVK LKVPGETQTG 300 KLFRMRGKGV KSVRGGAQGD LLCRVVVETP VGLNERQKQL LQELQESFGG PTGEHNSPRS 360 KSFFDGVKKF FDDLTR 376 |
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