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Database: UniProt
Entry: A0A3S4VUQ3_9ACTO
LinkDB: A0A3S4VUQ3_9ACTO
Original site: A0A3S4VUQ3_9ACTO 
ID   A0A3S4VUQ3_9ACTO        Unreviewed;       370 AA.
AC   A0A3S4VUQ3;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 15.
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:VEI14108.1};
GN   ORFNames=NCTC13354_01840 {ECO:0000313|EMBL:VEI14108.1};
OS   Trueperella bialowiezensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Trueperella.
OX   NCBI_TaxID=312285 {ECO:0000313|EMBL:VEI14108.1, ECO:0000313|Proteomes:UP000269542};
RN   [1] {ECO:0000313|EMBL:VEI14108.1, ECO:0000313|Proteomes:UP000269542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC13354 {ECO:0000313|EMBL:VEI14108.1,
RC   ECO:0000313|Proteomes:UP000269542};
RG   Pathogen Informatics;
RL   Submitted (DEC-2018) 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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01152}.
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DR   EMBL; LR134476; VEI14108.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3S4VUQ3; -.
DR   KEGG; tbw:NCTC13354_01840; -.
DR   OrthoDB; 9779889at2; -.
DR   Proteomes; UP000269542; 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   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   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|HAMAP-Rule:MF_01152};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01152}; Reference proteome {ECO:0000313|Proteomes:UP000269542};
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          3..66
FT                   /note="J"
FT                   /evidence="ECO:0000259|PROSITE:PS50076"
FT   DOMAIN          124..206
FT                   /note="CR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51188"
FT   ZN_FING         124..206
FT                   /note="CR-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
FT   BINDING         137
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01152"
FT   BINDING         140
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01152"
FT   BINDING         154
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01152"
FT   BINDING         157
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01152"
FT   BINDING         180
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01152"
FT   BINDING         183
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="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01152"
FT   BINDING         197
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01152"
SQ   SEQUENCE   370 AA;  39647 MW;  888A0D84C3155D8C CRC64;
     MADYYDILGV SRDATQAEIK KAYRKKARLL HPDEAGGGSE EEFKEVNKAY EVLSNEEKRQ
     LYDIGGEAAV SGNGLAAPGF GGFQDIFDTF FGGGNTRRGP ASRTRRGQDS LIRLNLTLSD
     VVFGADKEIN HDAVIECPNC HGHMTEPGTE PVPCTNCDGT GTTQRMTQSL FGQVMAQTTC
     GQCQGFGTVI VTPCGECSGE GRVRANQNVT IKVPAGVENG MRIRLAGRGD AGIAGGPAGD
     LFAEVQIAPD PVFTRDGDDL LCTLEVPMTS AALGAHTEID TLDGTQTVEL KPGTQSGHVI
     KLPHLGVGRI HRGGRGDLKV HIQVATPTKL DSGQRELLEK FARMRGEDTP QLVQTTSSVF
     SRLKERFTSR
//
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