DNAJ_ACEP3
ID DNAJ_ACEP3 Reviewed; 380 AA.
AC Q75WD2; C7JC26;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Chaperone protein DnaJ {ECO:0000255|HAMAP-Rule:MF_01152};
GN Name=dnaJ {ECO:0000255|HAMAP-Rule:MF_01152}; OrderedLocusNames=APA01_02910;
OS Acetobacter pasteurianus (strain NBRC 105184 / IFO 3283-01).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acetobacter.
OX NCBI_TaxID=634452;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NBRC 105184 / IFO 3283-01;
RX PubMed=16233640; DOI=10.1016/s1389-1723(04)70216-9;
RA Okamoto-Kainuma A., Wan Y., Fukaya M., Tsukamoto Y., Ishikawa M.,
RA Koizumi Y.;
RT "Cloning and characterization of the dnaKJ operon in Acetobacter aceti.";
RL J. Biosci. Bioeng. 97:339-342(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 105184 / IFO 3283-01;
RX PubMed=19638423; DOI=10.1093/nar/gkp612;
RA Azuma Y., Hosoyama A., Matsutani M., Furuya N., Horikawa H., Harada T.,
RA Hirakawa H., Kuhara S., Matsushita K., Fujita N., Shirai M.;
RT "Whole-genome analyses reveal genetic instability of Acetobacter
RT pasteurianus.";
RL Nucleic Acids Res. 37:5768-5783(2009).
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; AB121676; BAD14920.1; -; Genomic_DNA.
DR EMBL; AP011121; BAH98443.1; -; Genomic_DNA.
DR RefSeq; WP_003623818.1; NC_013209.1.
DR AlphaFoldDB; Q75WD2; -.
DR SMR; Q75WD2; -.
DR STRING; 634452.APA01_02910; -.
DR EnsemblBacteria; BAH98443; BAH98443; APA01_02910.
DR GeneID; 60375625; -.
DR KEGG; apt:APA01_02910; -.
DR eggNOG; COG0484; Bacteria.
DR HOGENOM; CLU_017633_0_7_5; -.
DR OMA; DLHCTVT; -.
DR BioCyc; APAS634452:APA01_RS01465-MON; -.
DR Proteomes; UP000000948; 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; cd10719; DnaJ_zf; 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; Reference proteome;
KW Repeat; Stress response; Zinc; Zinc-finger.
FT CHAIN 1..380
FT /note="Chaperone protein DnaJ"
FT /id="PRO_0000070703"
FT DOMAIN 6..71
FT /note="J"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT REPEAT 149..156
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 136..215
FT /note="CR-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 152
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"
FT CONFLICT 88
FT /note="G -> S (in Ref. 1; BAD14920)"
FT /evidence="ECO:0000305"
FT CONFLICT 146..151
FT /note="RVACEA -> LGVRT (in Ref. 1; BAD14920)"
FT /evidence="ECO:0000305"
FT CONFLICT 179..180
FT /note="QQ -> HE (in Ref. 1; BAD14920)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="V -> F (in Ref. 1; BAD14920)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="L -> F (in Ref. 1; BAD14920)"
FT /evidence="ECO:0000305"
FT CONFLICT 309..311
FT /note="HFR -> TFS (in Ref. 1; BAD14920)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 380 AA; 41177 MW; 72F46502E04EFA34 CRC64;
MATQLDYYAI LEVSRTATAD ELKKSYRKLA MKYHPDRNPG DDAAEAKFKE INQAYDILKD
EQKRAAYDQY GHAAFEGGGP GPGGFDFGGG FGGGGLGDIF EQMFGDMMGG RRGGRARTGN
DIQTHVEITL EEAFSGVKKD VRVITRVACE ACHGTGSDDG ASGVEVCPSC HGAGKVRAQQ
GFFVVERPCP TCHGAGKVVK NPCKVCHGEG TVEKERTVEV QIPAGVEDGT RIRLSGEGEA
GGNGVPPGDL YIHVSVTEHG IFQRDGANIY CRVPLRMAQA ALGTEIEVPV IDGSRTKVKI
PAGTQTGAHF RLRGKGFSVL RSTARGDMYI QVTVETPQNL SKRQRELLEE FEKEAGEDVK
QSPEHTGFFR RVRDFFEGKE
