ID B6BWR5_9PROT Unreviewed; 377 AA.
AC B6BWR5;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 24-JAN-2024, entry version 86.
DE RecName: Full=Chaperone protein DnaJ {ECO:0000256|HAMAP-Rule:MF_01152};
GN Name=dnaJ {ECO:0000256|HAMAP-Rule:MF_01152,
GN ECO:0000313|EMBL:EDZ64795.1};
GN ORFNames=KB13_927 {ECO:0000313|EMBL:EDZ64795.1};
OS beta proteobacterium KB13.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales; OM43 clade.
OX NCBI_TaxID=314607 {ECO:0000313|EMBL:EDZ64795.1, ECO:0000313|Proteomes:UP000004188};
RN [1] {ECO:0000313|Proteomes:UP000004188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KB13 {ECO:0000313|Proteomes:UP000004188};
RX PubMed=22675594; DOI=10.4056/sigs.2305090;
RA Huggett M.J., Hayakawa D.H., Rappe M.S.;
RT "Genome sequence of strain HIMB624, a cultured representative from the OM43
RT clade of marine Betaproteobacteria.";
RL Stand. Genomic Sci. 6:11-20(2012).
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:0000256|HAMAP-Rule:MF_01152}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01152};
CC Note=Binds 2 Zn(2+) ions per monomer. {ECO:0000256|HAMAP-
CC Rule:MF_01152};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01152}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_01152}.
CC -!- SIMILARITY: Belongs to the DnaJ family. {ECO:0000256|HAMAP-
CC Rule:MF_01152}.
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DR EMBL; DS995299; EDZ64795.1; -; Genomic_DNA.
DR AlphaFoldDB; B6BWR5; -.
DR STRING; 314607.KB13_927; -.
DR eggNOG; COG0484; Bacteria.
DR HOGENOM; CLU_017633_0_7_4; -.
DR Proteomes; UP000004188; Unassembled WGS sequence.
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 CDD; cd10747; DnaJ_C; 1.
DR CDD; cd10719; DnaJ_zf; 1.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR Gene3D; 2.10.230.10; Heat shock protein DnaJ, cysteine-rich domain; 1.
DR Gene3D; 2.60.260.20; Urease metallochaperone UreE, N-terminal domain; 2.
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 NCBIfam; TIGR02349; DnaJ_bact; 1.
DR PANTHER; PTHR43096:SF48; CHAPERONE PROTEIN DNAJ; 1.
DR PANTHER; PTHR43096; DNAJ HOMOLOG 1, MITOCHONDRIAL-RELATED; 1.
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; Chaperone J-domain; 1.
DR SUPFAM; SSF57938; DnaJ/Hsp40 cysteine-rich domain; 1.
DR SUPFAM; SSF49493; HSP40/DnaJ peptide-binding domain; 2.
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 {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_01152};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01152};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW Rule:MF_01152};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01152};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_01152};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_01152};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01152};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|HAMAP-
KW Rule:MF_01152}.
FT DOMAIN 6..71
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 137..215
FT /note="CR-type"
FT /evidence="ECO:0000259|PROSITE:PS51188"
FT REPEAT 150..157
FT /note="CXXCXGXG motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152"
FT REPEAT 167..174
FT /note="CXXCXGXG motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152"
FT REPEAT 189..196
FT /note="CXXCXGXG motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152"
FT REPEAT 203..210
FT /note="CXXCXGXG motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152"
FT ZN_FING 137..215
FT /note="CR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152"
FT BINDING 206
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152"
SQ SEQUENCE 377 AA; 40614 MW; 043EC177EB6759A3 CRC64;
MASKRDYYEI LGLNRDASGD EIKKAFKKLA MKFHPDRNPD NPKAEESFKE VKEAYEILSD
PQKKSAYDQF GHAGVDQSMG GGQGGFQGGF SDFGDAFGDI FGDIFGGGRS GSGKSNVYRG
ADLRYNLEIT LEEAAQGTEK KIRIPVLSQC KTCSGSGAKK GTQPSTCGTC GGHGQVRMQQ
GFFSVQQTCP KCQGSGKVIN DPCNDCSGSG RVKESKTLSV KIPAGVDEGD RIRLSNEGEA
GVNGGPSGDL YVVVGLKKHA IFERDGADLH CELPISFSVA ALGGDVEIPT LGGNAKMKIP
QETQTGATFR LKGKGVKPVR ENYTGDLLCH VVVETPVKLT ERQKEILREL EDLNQADSGK
HSPRSKSWVD KVRDFFD
//
