ACL_RS02765

Uniprot: A9NFN9
Description: molecular chaperone DnaJ
EC number:
Annotation score: 3 out of 5
Miscellaneous [CC]:
Protein existence: Inferred from homology
Catalytic activity:
Cofactor: COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-Rule:MF_01152}; ; Note=Binds 2 Zn(2+) ions per monomer. {ECO:0000256|HAMAP-Rule:MF_01152}
Enzyme regulation:
Function [CC]: FUNCTION: 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. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins. {ECO:0000256|HAMAP-Rule:MF_01152}.
Pathway:
Active site:
Binding site:
Calcium binding:
DNA binding:
Metal binding: METAL 144 144 Zinc 1. {ECO:0000256|HAMAP-Rule:MF_01152}.; METAL 147 147 Zinc 1. {ECO:0000256|HAMAP-Rule:MF_01152}.; METAL 161 161 Zinc 2. {ECO:0000256|HAMAP-Rule:MF_01152}.; METAL 164 164 Zinc 2. {ECO:0000256|HAMAP-Rule:MF_01152}.; METAL 187 187 Zinc 2. {ECO:0000256|HAMAP-Rule:MF_01152}.; METAL 190 190 Zinc 2. {ECO:0000256|HAMAP-Rule:MF_01152}.; METAL 201 201 Zinc 1. {ECO:0000256|HAMAP-Rule:MF_01152}.; METAL 204 204 Zinc 1. {ECO:0000256|HAMAP-Rule:MF_01152}.
Nucleotide binding:
Site:
Gene names (primary): dnaJ
Gene names (synonym):
Mass: 40,433
Subunit structure [CC]: SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01152}.
Gene ontology (GO): cytoplasm [GO:0005737]; ATP binding [GO:0005524]; zinc ion binding [GO:0008270]; DNA replication [GO:0006260]; protein folding [GO:0006457]; response to heat [GO:0009408]
Gene ontology IDs: GO:0005524; GO:0005737; GO:0006260; GO:0006457; GO:0008270; GO:0009408
Chain:
Signal peptide:
Domain [CC]: DOMAIN: The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity. {ECO:0000256|HAMAP-Rule:MF_01152}.
Sequence similarities: SIMILARITY: Belongs to the DnaJ family. {ECO:0000256|HAMAP-Rule:MF_01152}.; SIMILARITY: Contains 1 CR-type zinc finger. {ECO:0000256|HAMAP-Rule:MF_01152}.; SIMILARITY: Contains 1 J domain. {ECO:0000256|HAMAP-Rule:MF_01152}.
Protein families: DnaJ family
Coiled coil:
Domain [FT]: DOMAIN 5 69 J. {ECO:0000259|PROSITE:PS50076}.; DOMAIN 131 213 CR-type. {ECO:0000259|PROSITE:PS51188}.
Motif:
Region:
EMBL: CP000896
ProteinModelPortal: A9NFN9
MEROPS:
EnsemblBacteria KO: ABX81169
UniPathway: K03686
CDD:
Gene3D: cd06257
HAMAP: 1.10.287.110;2.10.230.10
InterPro: MF_01152
PANTHER: IPR012724;IPR002939;IPR001623;IPR018253;IPR008971;IPR001305
PIRSF:
PRINTS:
PROSITE: PR00625
Pfam: PS00636;PS50076;PS51188
ProDom: PF00226;PF01556;PF00684
SMART:
SUPFAM: SM00271
TIGRFAMs: SSF46565;SSF49493;SSF57938

587546-588656(+)

>nucleotide sequence
ATGGCAAAAAGAGATTATTATGATGTGCTAGGTATATCAAAAAGTGCATCTCAAGACGAA
ATTAAAAAAGCTTACAGAAGTTTAGCTAAAAAATATCACCCTGACGTTTCAAAGGAAAAA
GATGCTGAAACAAAATTTAAAGAAGTTCAAGAAGCCTATGATGTCTTAAATGATTCAAAT
AAAAAAGCACAATACGATAGATTTGGTCATGCTGGTACTGGACAAGATCCATTTGGTGGT
GCTGGTGGTGGTTTTGGCGGATTTGGTGGCTTTGATGACATTATTAGCCAATTCTTTGGT
GGTGGACAAACACGTAGAACACGTCAAACATCAAATGTTGGTGAAGACTTAAATATGCGT
ATGACCATCGATTTTATGGAAGCAGTTTTAGGTACAACAAAAAATGTTTCTGTAGATATC
ACTCAAGATTGTGGTCACTGTCATGGCTCTGGTGCAGAAAGTTCAAAAGACGTTCATACC
TGTAGCAAATGTCATGGTCAAGGATTTATTAACGTAGACCAACGTACCATGTTTGGTACA
ATGAGAAGTCAACAAGTATGTCCACAATGTCAAGGTGAAGGGCAAACAATTGATAACAAA
TGTCATGTTTGTTCCGGTGCTGGACGTGTTAAGGCTAAAAAGACAGTGGATGTGAAAGTA
CCTGCTGGTGTCGATAATGAAATGACATTACGCGTACCAGGTTATGGTAATGGTGGTAGA
AAAGGTGCTGAATCAGGTGACCTATACATCACATTTAGAGTGAAACCACATAAAATATTT
AAACGTCGTGGTTCAGATATCATTTTAGATGTACCTATTACATTTACGCAAGCTGCACTT
GGAGACAAAATTGATATACCAACTATTTATGGTGAAGTAGAGTTAACCATACCTGCAGGT
ATTCAATCTGGTACTGAACTTAAATTAAAAAATAAGGGAACAAAAGATCCAAGAACTGGT
AAGACAGGTGATCAACATGTTATCGTCAATATTGAGACACCTAAAAACTTATCTAGTGAG
GAAAAGAAATTATTTGAACAGTTAAGTAAACTGGATTCCCCAAGAAAGAAATCTGGTTGG
GATAAATTCAAATCATTCTTTACAAATTAA

>protein sequence
MAKRDYYDVLGISKSASQDEIKKAYRSLAKKYHPDVSKEKDAETKFKEVQEAYDVLNDSN
KKAQYDRFGHAGTGQDPFGGAGGGFGGFGGFDDIISQFFGGGQTRRTRQTSNVGEDLNMR
MTIDFMEAVLGTTKNVSVDITQDCGHCHGSGAESSKDVHTCSKCHGQGFINVDQRTMFGT
MRSQQVCPQCQGEGQTIDNKCHVCSGAGRVKAKKTVDVKVPAGVDNEMTLRVPGYGNGGR
KGAESGDLYITFRVKPHKIFKRRGSDIILDVPITFTQAALGDKIDIPTIYGEVELTIPAG
IQSGTELKLKNKGTKDPRTGKTGDQHVIVNIETPKNLSSEEKKLFEQLSKLDSPRKKSGW
DKFKSFFTN