ID A0A0X8GZS7_9FIRM Unreviewed; 371 AA.
AC A0A0X8GZS7;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Chaperone protein DnaJ {ECO:0000256|HAMAP-Rule:MF_01152};
GN Name=dnaJ {ECO:0000256|HAMAP-Rule:MF_01152};
GN ORFNames=AOC36_05465 {ECO:0000313|EMBL:AMC93447.1};
OS Erysipelothrix larvae.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Erysipelothrix.
OX NCBI_TaxID=1514105 {ECO:0000313|EMBL:AMC93447.1, ECO:0000313|Proteomes:UP000063781};
RN [1] {ECO:0000313|EMBL:AMC93447.1, ECO:0000313|Proteomes:UP000063781}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LV19 {ECO:0000313|EMBL:AMC93447.1,
RC ECO:0000313|Proteomes:UP000063781};
RA Lim S., Kim B.-C.;
RT "Erysipelothrix larvae sp. LV19 isolated from the larval gut of the
RT rhinoceros beetle, Trypoxylus dichotomus.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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; CP013213; AMC93447.1; -; Genomic_DNA.
DR RefSeq; WP_067632244.1; NZ_CP013213.1.
DR AlphaFoldDB; A0A0X8GZS7; -.
DR STRING; 1514105.AOC36_05465; -.
DR KEGG; erl:AOC36_05465; -.
DR OrthoDB; 9779889at2; -.
DR Proteomes; UP000063781; Chromosome.
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; 6.20.20.10; -; 2.
DR Gene3D; 1.10.287.110; DnaJ 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; DNAJ HOMOLOG 1, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR43096:SF52; 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|HAMAP-Rule:MF_01152};
KW Cytoplasm {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}; Reference proteome {ECO:0000313|Proteomes:UP000063781};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_01152};
KW Stress response {ECO:0000256|HAMAP-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..70
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 135..217
FT /note="CR-type"
FT /evidence="ECO:0000259|PROSITE:PS51188"
FT REPEAT 148..155
FT /note="CXXCXGXG motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152"
FT REPEAT 165..172
FT /note="CXXCXGXG motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152"
FT REPEAT 191..198
FT /note="CXXCXGXG motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152"
FT REPEAT 205..212
FT /note="CXXCXGXG motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152"
FT ZN_FING 135..217
FT /note="CR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152"
FT BINDING 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152"
SQ SEQUENCE 371 AA; 40431 MW; D2CEC0A23385FCC7 CRC64;
MAQKKDYYEI LGVNKSASDA EIKKAYRKLA KQYHPDVNKS EDASEKFKEV QEAYDILSDS
TKRAQYDQYG HAAFDQSGGF GGGAGFDMGD IFSQFFGGGF GGGFGGGSRR TASGPRQGDN
RFMTMRIDFM EAVFGVDKTV KMTVDETCTV CHGSGAHSRE DIKTCSRCGG SGHVTTQQRT
PFGVFESTGV CPDCSGTGKT IARKCENCHG HGYVSKRVDV EIHVPAGIVS GQQLRVSGKG
ERGANGGPNG DLYVEIVVNP HKHFVREGNN INVSIPISAV DAILGTQVDV PTVHGDVSLT
IPAGTQPNTR FRLRGKGVKD LRSDNYGDQY VEVKVEVPKK LNREEKSLFE KIKQAEGKND
SVFERFKKNF K
//
