CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
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
31AYKRLAMKYHPDRNQacetylation[1]
41PDRNQGDKEAEAKFKacetylation[1]
46GDKEAEAKFKEIKEAacetylation[1]
51EAKFKEIKEAYEVLTacetylation[1]
62EVLTDSQKRAAYDQYacetylation[1]
194QGRGTLIKDPCNKCHacetylation[2]
215RSKTLSVKIPAGVDTacetylation[1]
292LDGRVKLKVPGETQTacetylation[1]
301PGETQTGKLFRMRGKacetylation[1]
361EHNSPRSKSFFDGVKacetylation[1]
368KSFFDGVKKFFDDLTacetylation[1]
369SFFDGVKKFFDDLTRacetylation[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]
 [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 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:EcoliWiki.
 GO:0016020; C:membrane; IDA:EcoliWiki.
 GO:0005524; F:ATP binding; IEA:InterPro.
 GO:0003756; F:protein disulfide isomerase activity; IDA:EcoliWiki.
 GO:0051082; F:unfolded protein binding; IDA:EcoliWiki.
 GO:0008270; F:zinc ion binding; IDA:EcoliWiki.
 GO:0006260; P:DNA replication; IMP:EcoliWiki.
 GO:0042026; P:protein refolding; IDA:EcoliWiki.
 GO:0043335; P:protein unfolding; IDA:EcoCyc.
 GO:0009408; P:response to heat; IEP:EcoliWiki. 
Interpro
 IPR012724; DnaJ.
 IPR002939; DnaJ_C.
 IPR001623; DnaJ_domain.
 IPR018253; DnaJ_domain_CS.
 IPR008971; HSP40/DnaJ_pept-bd.
 IPR001305; HSP_DnaJ_Cys-rich_dom. 
Pfam
 PF00226; DnaJ
 PF01556; DnaJ_C
 PF00684; DnaJ_CXXCXGXG 
SMART
 SM00271; DnaJ 
PROSITE
 PS00636; DNAJ_1
 PS50076; DNAJ_2
 PS51188; ZF_CR 
PRINTS
 PR00625; JDOMAIN.