GCW_00845

Uniprot: A0A0F6CK44
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 158 158 Zinc 1. {ECO:0000256|HAMAP-Rule:MF_01152}.; METAL 161 161 Zinc 1. {ECO:0000256|HAMAP-Rule:MF_01152}.; METAL 174 174 Zinc 2. {ECO:0000256|HAMAP-Rule:MF_01152}.; METAL 177 177 Zinc 2. {ECO:0000256|HAMAP-Rule:MF_01152}.; METAL 200 200 Zinc 2. {ECO:0000256|HAMAP-Rule:MF_01152}.; METAL 203 203 Zinc 2. {ECO:0000256|HAMAP-Rule:MF_01152}.; METAL 214 214 Zinc 1. {ECO:0000256|HAMAP-Rule:MF_01152}.; METAL 217 217 Zinc 1. {ECO:0000256|HAMAP-Rule:MF_01152}.
Nucleotide binding:
Site:
Gene names (primary): dnaJ_2
Gene names (synonym): dnaJ
Mass: 44,038
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 6 70 J. {ECO:0000259|PROSITE:PS50076}.; DOMAIN 145 226 CR-type. {ECO:0000259|PROSITE:PS51188}.
Motif:
Region:
EMBL: CP006916
ProteinModelPortal: A0A0F6CK44
MEROPS:
EnsemblBacteria KO: AHB99466
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
187599-188775(-)

>nucleotide sequence
TTATTGCGAATTCTTATTATTAAGTTCTTTCTTCATTAAGGTTTCGTATAAGTTTACTTC
CTTATTTGGTTTAATGAACTCTTTAAGTTTAGCAATCTCTTGTTTAGAGTATTCACTAGG
TCTTGCATAGTTGATTACAACGATTAGATCACCTTTTTGGTTGTAATTAGCCCCATAAAC
CCGTGAGTCTAGTTTTAAGTTAATTCCACCATTAGCGATCGTGATGATGTCACCGTTTTT
AGTTCCGGCTTTTAGATTAATCTCTTTGATCTCTTTTAAAGTCGGAATTAAGATTGTTCC
ACCAGTGATAGCCACCAATGGATCCACTAGAACATTAACCACCACGTGGTTATCGCGTAG
TTCAAACACCCTAGAAGGTTCGATCTTCACTCTTAAGAAAAGATCCCCCACTAGATTCTT
ATAAATGTGTCCTTCCCCGCGAACGATTACGACATCTTGATAAAAGACATTTGAATCGAT
TGAGACCTTTCTTTCAACGACTTCATCAACCATTCTACGTGATTTACATTTCTTACATTT
ATTTTTGATCGTTTGACCTTCACCTTTACAAGAAGGACAGGTCTTTTTGGTTTGGAACAT
TCCTAGTAATGTTCTTCTTTGTTCAACAACAAACCCTTCGCCATTACAATCACTACATGT
AATTACATCACCATCAGCTGAACCTGACCCGTTACAATCCGGACAAGTAACTTGTCTGGT
ATACTTAACATTTTTAATACAACCATTGGCCGCTTCTAAGAAGTTGATCTTAATCTCATG
AACTAAATTAACATCAACTTCTTCAATGTATTCTTGGTTGTGAAAACCACTGCCTCCACC
ACCAAAGAATTGTGAGAAAACATCACCAAACCCACCTTCGAAATCAAACCCGCTAAATAC
AGAGTTAAACACGTCATAAGGATTGAATCCACCTTGGTGGAATCCAGACGCGTTTAAACC
TTCATGACCATAAGTGTCATAAAGTTTTCTTTTCTCTTCATCGCTTAGTACCTCGTAAGC
TTCATTAACTTCTTTGAACTTTTCTTCAGCATCTGAATCTTTATTGCGATCGGGGTGATA
TTTCATAGCCAGTTTTCTAAAGGCTTTTTTAATATCTTGCTGGGTAGCTGAACGGGATAC
TTCTAATATTTCGTAATAATCTCTTTTTGAAGACAT

>protein sequence
MSSKRDYYEILEVSRSATQQDIKKAFRKLAMKYHPDRNKDSDAEEKFKEVNEAYEVLSDE
EKRKLYDTYGHEGLNASGFHQGGFNPYDVFNSVFSGFDFEGGFGDVFSQFFGGGGSGFHN
QEYIEEVDVNLVHEIKINFLEAANGCIKNVKYTRQVTCPDCNGSGSADGDVITCSDCNGE
GFVVEQRRTLLGMFQTKKTCPSCKGEGQTIKNKCKKCKSRRMVDEVVERKVSIDSNVFYQ
DVVIVRGEGHIYKNLVGDLFLRVKIEPSRVFELRDNHVVVNVLVDPLVAITGGTILIPTL
KEIKEINLKAGTKNGDIITIANGGINLKLDSRVYGANYNQKGDLIVVINYARPSEYSKQE
IAKLKEFIKPNKEVNLYETLMKKELNNKNSQ