ID D7DWD9_NOSA0 Unreviewed; 378 AA.
AC D7DWD9;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Chaperone protein DnaJ {ECO:0000256|HAMAP-Rule:MF_01152};
GN Name=dnaJ {ECO:0000256|HAMAP-Rule:MF_01152};
GN OrderedLocusNames=Aazo_1980 {ECO:0000313|EMBL:ADI64056.1};
OS Nostoc azollae (strain 0708) (Anabaena azollae (strain 0708)).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae;
OC Trichormus.
OX NCBI_TaxID=551115 {ECO:0000313|EMBL:ADI64056.1, ECO:0000313|Proteomes:UP000001511};
RN [1] {ECO:0000313|EMBL:ADI64056.1, ECO:0000313|Proteomes:UP000001511}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0708 {ECO:0000313|EMBL:ADI64056.1,
RC ECO:0000313|Proteomes:UP000001511};
RX PubMed=20628610; DOI=10.1371/journal.pone.0011486;
RA Ran L., Larsson J., Vigil-Stenman T., Nylander J.A., Ininbergs K.,
RA Zheng W.W., Lapidus A., Lowry S., Haselkorn R., Bergman B.;
RT "Genome erosion in a nitrogen-fixing vertically transmitted endosymbiotic
RT multicellular cyanobacterium.";
RL PLoS ONE 5:E11486-E11486(2010).
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; CP002059; ADI64056.1; -; Genomic_DNA.
DR RefSeq; WP_013191073.1; NC_014248.1.
DR AlphaFoldDB; D7DWD9; -.
DR STRING; 551115.Aazo_1980; -.
DR KEGG; naz:Aazo_1980; -.
DR eggNOG; COG0484; Bacteria.
DR HOGENOM; CLU_017633_0_1_3; -.
DR OrthoDB; 9779889at2; -.
DR Proteomes; UP000001511; 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; 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; 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:SF10; CHAPERONE PROTEIN DNAJ A6, CHLOROPLASTIC; 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; 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:UP000001511};
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 4..68
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 138..220
FT /note="CR-type"
FT /evidence="ECO:0000259|PROSITE:PS51188"
FT REPEAT 151..158
FT /note="CXXCXGXG motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152"
FT REPEAT 168..175
FT /note="CXXCXGXG motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152"
FT REPEAT 194..201
FT /note="CXXCXGXG motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152"
FT REPEAT 208..215
FT /note="CXXCXGXG motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152"
FT ZN_FING 138..220
FT /note="CR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
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 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
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 171
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 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
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"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152"
SQ SEQUENCE 378 AA; 41165 MW; C08F57C518964388 CRC64;
MARDYYEILG VSRDADKEEI KQAYRRQARK YHPDVNKEPG SEEQFKEINR AYEVLSEPET
RERYNRFGEA GVSGAAAGAG FQDMGDMGGF ADIFESIFSG FAGGMGSPTQ QQRRRSGPVR
GDDLRLDLKL DFREAVFGGE KEIRISHLET CEVCSGSGAK PGTRPRSCAT CSGSGQVRRV
TRTPFGSFTQ VSTCPTCNGT GTVVEDKCDA CDGKGANQVT KKLKITIPAG VDNGTRLRIS
QEGDAGQRGG PAGDLYVYLF VNEDEEFQRD GINVLSEIKI SYLQAILGCR LEVNTVDGPV
ELIIPAGTQP NTVMKLENRG VPRLGNPVSR GDHMLTVLID IPNKIAPEER QLLEQLAKIK
GDRTGKGGIE GFLGSLFK
//
