DNAJ_CUPTR
ID DNAJ_CUPTR Reviewed; 377 AA.
AC B3R6G6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Chaperone protein DnaJ {ECO:0000255|HAMAP-Rule:MF_01152};
GN Name=dnaJ {ECO:0000255|HAMAP-Rule:MF_01152}; OrderedLocusNames=RALTA_A2563;
OS Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CCUG 44338 / CIP
OS 107171 / LMG 19424 / R1) (Ralstonia taiwanensis (strain LMG 19424)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=977880;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17343 / BCRC 17206 / CCUG 44338 / CIP 107171 / LMG 19424 / R1;
RX PubMed=18490699; DOI=10.1101/gr.076448.108;
RA Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D.,
RA Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V.,
RA Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C.,
RA Masson-Boivin C.;
RT "Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and
RT comparative genomics of rhizobia.";
RL Genome Res. 18:1472-1483(2008).
CC -!- FUNCTION: Participates actively in the response to hyperosmotic and
CC heat shock by preventing the aggregation of stress-denatured proteins
CC and by disaggregating proteins, also in an autonomous, DnaK-independent
CC fashion. Unfolded proteins bind initially to DnaJ; upon interaction
CC with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting
CC in the formation of a stable complex. GrpE releases ADP from DnaK; ATP
CC binding to DnaK triggers the release of the substrate protein, thus
CC completing the reaction cycle. Several rounds of ATP-dependent
CC interactions between DnaJ, DnaK and GrpE are required for fully
CC efficient folding. Also involved, together with DnaK and GrpE, in the
CC DNA replication of plasmids through activation of initiation proteins.
CC {ECO:0000255|HAMAP-Rule:MF_01152}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01152};
CC Note=Binds 2 Zn(2+) ions per monomer. {ECO:0000255|HAMAP-
CC Rule:MF_01152};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01152}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01152}.
CC -!- DOMAIN: The J domain is necessary and sufficient to stimulate DnaK
CC ATPase activity. Zinc center 1 plays an important role in the
CC autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2
CC is essential for interaction with DnaK and for DnaJ activity.
CC {ECO:0000255|HAMAP-Rule:MF_01152}.
CC -!- SIMILARITY: Belongs to the DnaJ family. {ECO:0000255|HAMAP-
CC Rule:MF_01152}.
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DR EMBL; CU633749; CAQ70494.1; -; Genomic_DNA.
DR RefSeq; WP_012353790.1; NC_010528.1.
DR AlphaFoldDB; B3R6G6; -.
DR SMR; B3R6G6; -.
DR STRING; 977880.RALTA_A2563; -.
DR EnsemblBacteria; CAQ70494; CAQ70494; RALTA_A2563.
DR GeneID; 29761325; -.
DR KEGG; cti:RALTA_A2563; -.
DR eggNOG; COG0484; Bacteria.
DR HOGENOM; CLU_017633_0_7_4; -.
DR OMA; DLHCTVT; -.
DR OrthoDB; 1738789at2; -.
DR BioCyc; CTAI977880:RALTA_RS12465-MON; -.
DR Proteomes; UP000001692; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0031072; F:heat shock protein binding; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0009408; P:response to heat; IEA:InterPro.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR HAMAP; MF_01152; DnaJ; 1.
DR InterPro; IPR012724; DnaJ.
DR InterPro; IPR002939; DnaJ_C.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR InterPro; IPR001305; HSP_DnaJ_Cys-rich_dom.
DR InterPro; IPR036410; HSP_DnaJ_Cys-rich_dom_sf.
DR InterPro; IPR036869; J_dom_sf.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF01556; DnaJ_C; 1.
DR Pfam; PF00684; DnaJ_CXXCXGXG; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF49493; SSF49493; 2.
DR SUPFAM; SSF57938; SSF57938; 1.
DR TIGRFAMs; TIGR02349; DnaJ_bact; 1.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51188; ZF_CR; 1.
PE 3: Inferred from homology;
KW Chaperone; Cytoplasm; DNA replication; Metal-binding; Repeat;
KW Stress response; Zinc; Zinc-finger.
FT CHAIN 1..377
FT /note="Chaperone protein DnaJ"
FT /id="PRO_1000137675"
FT DOMAIN 5..70
FT /note="J"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT REPEAT 150..157
FT /note="CXXCXGXG motif"
FT REPEAT 167..174
FT /note="CXXCXGXG motif"
FT REPEAT 189..196
FT /note="CXXCXGXG motif"
FT REPEAT 203..210
FT /note="CXXCXGXG motif"
FT ZN_FING 137..215
FT /note="CR-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 206
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
SQ SEQUENCE 377 AA; 40806 MW; 7399C47C2EA95FDB CRC64;
MAKRDYYEVL GVGKNASDDE IKKAYRKLAM KFHPDRNPDS KDAEEKFKEA KEAYEMLSDP
EKKAAYDQYG HAGVDPNMAG GFGGAQGYGG FAEAFGDIFG DIFGQGGGGR RGGGPQAYRG
ADLRYSMEIS LEQAAHGHEA QIRVPHWDDC DHCHGNGAEP GSSVETCPTC HGAGQVRVSQ
GFFTMQQTCP KCHGSGKFIP KPCTKCHGQG KLKSQKTLEV KIPAGIDEGM RIRSSGNGEP
GINGGPPGDL YVEVHIKPHA VFERDGDDLH CQMPISFATA ALGGDLEVPT LSGKATFPVP
EATQSGKTFR LRGKGIKGVR SGYPGDLYVH VNVETPVKLT EAQKEMLRQF DRSVHEGGSR
HSPQETSWLD KVKSFFS
