DNAJ1_STRCO
ID DNAJ1_STRCO Reviewed; 399 AA.
AC P40170;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Chaperone protein DnaJ 1 {ECO:0000255|HAMAP-Rule:MF_01152};
GN Name=dnaJ1 {ECO:0000255|HAMAP-Rule:MF_01152}; OrderedLocusNames=SCO3669;
GN ORFNames=SCH44.09c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A3(2) / NRRL B-16638;
RX PubMed=8801421; DOI=10.1111/j.1365-2958.1995.mmi_17040663.x;
RA Bucca G., Ferina G., Puglia A.M., Smith C.P.;
RT "The dnaK operon of Streptomyces coelicolor encodes a novel heat-shock
RT protein which binds to the promoter region of the operon.";
RL Mol. Microbiol. 17:663-674(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-387.
RC STRAIN=A3(2) / NRRL B-16638;
RX PubMed=8722574; DOI=10.3109/10425179609010207;
RA Brans A., Loriaux A., Joris B., Dusart J.;
RT "Cloning and sequencing of the dnaK locus in Streptomyces coelicolor
RT A3(2).";
RL DNA Seq. 6:179-184(1996).
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; L46700; AAB29453.1; -; Genomic_DNA.
DR EMBL; AL939117; CAB91160.1; -; Genomic_DNA.
DR EMBL; X77458; CAA54608.1; -; Genomic_DNA.
DR PIR; S41948; S41948.
DR PIR; S70206; S70206.
DR RefSeq; NP_627862.1; NC_003888.3.
DR RefSeq; WP_003975270.1; NZ_VNID01000003.1.
DR AlphaFoldDB; P40170; -.
DR SMR; P40170; -.
DR STRING; 100226.SCO3669; -.
DR GeneID; 1099105; -.
DR KEGG; sco:SCO3669; -.
DR PATRIC; fig|100226.15.peg.3727; -.
DR eggNOG; COG0484; Bacteria.
DR HOGENOM; CLU_017633_0_6_11; -.
DR InParanoid; P40170; -.
DR OMA; RVCPTCV; -.
DR PhylomeDB; P40170; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
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..399
FT /note="Chaperone protein DnaJ 1"
FT /id="PRO_0000070898"
FT DOMAIN 10..75
FT /note="J"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT REPEAT 179..186
FT /note="CXXCXGXG motif"
FT REPEAT 195..202
FT /note="CXXCXGXG motif"
FT REPEAT 218..225
FT /note="CXXCXGXG motif"
FT REPEAT 232..239
FT /note="CXXCXGXG motif"
FT ZN_FING 166..244
FT /note="CR-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 198
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 218
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT CONFLICT 278
FT /note="D -> H (in Ref. 1; AAB29453)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 399 AA; 41337 MW; 4C7A3412B61B3F12 CRC64;
MSTKDFIEKD YYKVLGVPKD ATEAEIKKAY RKLARENHPD ANKGNVKAEE RFKEISEAND
ILGDPKKRKE YDEARALFGN GGFRPGPGAG GGGTFNFDLG DLFGGGAQGG GGQGGAGGFG
GGLGDVFGGL FNRTGGGPGT GTRTQPRRGQ DIESEVTLSF TEAIEGATVP LRMSSQAPCK
ACSGTGDKNG TPRVCPTCVG TGQVARGSGG GFSLTDPCPD CKGRGLIAED PCEVCKGSGR
AKSSRTMQVR IPAGVSDGQR IRLRGKGTPG ERGGPAGDLY VVVHVKEHPV FGRRGDNLTV
TVPVTYAEAA LGGEVRVPTL GGPSVTLKLP AGTPNGRTMR ARGKGAVRKD GTRGDLLVTV
EVSVPKDLTG KARDALQAYR EATADEDPRA ELFQAAKGA
