SPM_001425

Uniprot: A0A037ULH4
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 156 156 Zinc 1. {ECO:0000256|HAMAP-Rule:MF_01152}.; METAL 159 159 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
Gene names (synonym):
Mass: 42,503
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 143 226 CR-type. {ECO:0000259|PROSITE:PS51188}.
Motif:
Region:
EMBL: AGBZ02000001
ProteinModelPortal:
MEROPS:
EnsemblBacteria KO: KAI92719
UniPathway:
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

260262-261399(-)

>nucleotide sequence
TTATAAATCTTCATAAAAATCATCAGTAATTTTAAACGAACTATTATTTCTTAACTTTTG
TAAAATTGTTTTTTCTTCTGGCGATAATTTTGTTGGAATTGTTACAATCACATTAACAAT
TAAGTCTCCCCGTTTGGTTGATGTTGGTGACTTGAAAAACCCATGATTTGGAATATTAAA
AATACTATTTGTTTTTGTATTTGGTGGTAATTTCAAATGAACATCCCCATCAAAAGTTGG
AACTTTAACTTCAGCTCCTAGTAAAGCATCTAAATAAGATACTGGTAAATTTAAATGAAG
GTTATCATTAACTCGTTTAAAATATTTATTTGGTTTTACTGAAATTTCTAAATAAATATC
CCCTCGTGGACCATTATTTAAACCGTAGTTTCCTTTTTCTCGAATTCGTAATTGTTGATT
TTCATAAATTGATTTTGGTAAATCAATTTCTACTGTTTCTTTACCTCGATAATTTCCTTG
CCCTTTACATTTTGAACATTTATTGGTAATTACTTTTCCTCGCCCTTTACAGTCAGGACA
TGGTTGTTGTGATTGAATCACACCAAAAAGACTACGTTGTTCTAGGTTAATATAACCATA
CCCATCACAAGTTGTACAAGTATGAATGTCTTTTTTAGGATCTTTTGCCCCAGTTCCATC
ACACATTTCACATTTTTTATCAATATTTAAATCTAAGTTTATTTTTTTCCCAAACATTTG
TTCTTTTAACGTTAATGTAACACGGGCAGCAATATTTTCCCCTTTAATTGGCTGATTACT
AAAACCACGGCGTTTTTTACCACCACCAAAAAAGTTTTCAAAAATATCACCAAAACCACC
AAAACCACCAGAGAAAATATCTTCAAAATCTCCAGTACTACTAAAACCATGACTAAAGCC
ACCAAAGCCGTTAGGGTCAGTTCCAGCATGACCAAACTGATCATAATTACGGCGTTTATT
TGGATCAGATAAAACTTCATAAGCTTCATTAATTTCCTTAAACTTTGCTTCGGCATCTTT
TTCTTTTGAAACATCAGGGTGATATTTTTTTGCTAATTGTCGAAAAGCACGTTTAATTTC
ATCATCAGTGGCATTACGATTAACGCCCAATACTTCATAATAGTCTCGTTTTCCCAT

>protein sequence
MGKRDYYEVLGVNRNATDDEIKRAFRQLAKKYHPDVSKEKDAEAKFKEINEAYEVLSDPN
KRRNYDQFGHAGTDPNGFGGFSHGFSSTGDFEDIFSGGFGGFGDIFENFFGGGKKRRGFS
NQPIKGENIAARVTLTLKEQMFGKKINLDLNIDKKCEMCDGTGAKDPKKDIHTCTTCDGY
GYINLEQRSLFGVIQSQQPCPDCKGRGKVITNKCSKCKGQGNYRGKETVEIDLPKSIYEN
QQLRIREKGNYGLNNGPRGDIYLEISVKPNKYFKRVNDNLHLNLPVSYLDALLGAEVKVP
TFDGDVHLKLPPNTKTNSIFNIPNHGFFKSPTSTKRGDLIVNVIVTIPTKLSPEEKTILQ
KLRNNSSFKITDDFYEDL