DNAJ_RHIRD
ID DNAJ_RHIRD Reviewed; 379 AA.
AC Q6RSN5;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Chaperone protein DnaJ;
GN Name=dnaJ;
OS Rhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium
OS radiobacter).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=358;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF TYR-7; LEU-10;
RP GLU-20; LYS-22; ARG-26; LYS-27; TYR-32; HIS-33; ASP-35; LYS-46; PHE-47;
RP LYS-48; ALA-53; LEU-57; ASP-59; LYS-62; ARG-63; TYR-66 AND ASP-67.
RC STRAIN=RUOR;
RX PubMed=15381160; DOI=10.1016/j.biocel.2004.06.009;
RA Hennessy F., Boshoff A., Blatch G.L.;
RT "Rational mutagenesis of a 40 kDa heat shock protein from Agrobacterium
RT tumefaciens identifies amino acid residues critical to its in vivo
RT function.";
RL Int. J. Biochem. Cell Biol. 37:177-191(2005).
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 (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per monomer. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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 (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DnaJ family. {ECO:0000305}.
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DR EMBL; AY494599; AAR84666.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6RSN5; -.
DR SMR; Q6RSN5; -.
DR STRING; 1082932.ATCR1_16413; -.
DR eggNOG; COG0484; Bacteria.
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 1: Evidence at protein level;
KW Chaperone; Cytoplasm; DNA replication; Metal-binding; Repeat;
KW Stress response; Zinc; Zinc-finger.
FT CHAIN 1..379
FT /note="Chaperone protein DnaJ"
FT /id="PRO_0000070707"
FT DOMAIN 5..70
FT /note="J"
FT REPEAT 153..160
FT /note="CXXCXGXG motif"
FT REPEAT 170..177
FT /note="CXXCXGXG motif"
FT REPEAT 192..199
FT /note="CXXCXGXG motif"
FT REPEAT 206..213
FT /note="CXXCXGXG motif"
FT ZN_FING 140..218
FT /note="CR-type"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 206
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MUTAGEN 7
FT /note="Y->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:15381160"
FT MUTAGEN 10
FT /note="L->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:15381160"
FT MUTAGEN 20
FT /note="E->A: No effect."
FT /evidence="ECO:0000269|PubMed:15381160"
FT MUTAGEN 22
FT /note="K->A: No effect."
FT /evidence="ECO:0000269|PubMed:15381160"
FT MUTAGEN 26
FT /note="R->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:15381160"
FT MUTAGEN 27
FT /note="K->A: No effect."
FT /evidence="ECO:0000269|PubMed:15381160"
FT MUTAGEN 32
FT /note="Y->A: No effect."
FT /evidence="ECO:0000269|PubMed:15381160"
FT MUTAGEN 33
FT /note="H->Q: Loss of ability to grow at 40 degrees
FT Celsius."
FT /evidence="ECO:0000269|PubMed:15381160"
FT MUTAGEN 35
FT /note="D->E: Loss of ability to grow at 40 degrees
FT Celsius."
FT /evidence="ECO:0000269|PubMed:15381160"
FT MUTAGEN 46
FT /note="K->T: No effect."
FT /evidence="ECO:0000269|PubMed:15381160"
FT MUTAGEN 47
FT /note="F->L: No effect."
FT /evidence="ECO:0000269|PubMed:15381160"
FT MUTAGEN 48
FT /note="K->T: Slight decrease in function."
FT /evidence="ECO:0000269|PubMed:15381160"
FT MUTAGEN 53
FT /note="A->S: No effect."
FT /evidence="ECO:0000269|PubMed:15381160"
FT MUTAGEN 57
FT /note="L->S: Loss of function."
FT /evidence="ECO:0000269|PubMed:15381160"
FT MUTAGEN 59
FT /note="D->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:15381160"
FT MUTAGEN 59
FT /note="D->N: No effect."
FT /evidence="ECO:0000269|PubMed:15381160"
FT MUTAGEN 62
FT /note="K->A: No effect."
FT /evidence="ECO:0000269|PubMed:15381160"
FT MUTAGEN 63
FT /note="R->A: Great decrease in function."
FT /evidence="ECO:0000269|PubMed:15381160"
FT MUTAGEN 66
FT /note="Y->A: No effect."
FT /evidence="ECO:0000269|PubMed:15381160"
FT MUTAGEN 67
FT /note="D->A,N: No effect."
FT /evidence="ECO:0000269|PubMed:15381160"
SQ SEQUENCE 379 AA; 41069 MW; 42A1B0B33AD41CAD CRC64;
MAKADFYETL GVSKTADEKE LKSAFRKLAM KYHPDKNPDD ADSERKFKEI NEAYETLKDP
QKRAAYDRFG HAAFENGGMG GGGGGFGGGG FANGGFSDIF EDIFGEMMGG GRARRSSGGR
ERGADLRYNM EITLEEAFTG KTAQIRVPTS ITCDVCSGSG AKPGTQPKTC ATCQGSGRVR
AAQGFFSVER TCPTCHGRGQ TISDPCGKCH GQGRVTEERS LSVNIPSGIE DGTRIRLQGE
GEAGMRGGPA GDLYIFLSVR PHEFFQRDGA DLYCTVPISM TTAALGGTFD VTTLDGTKSR
VTVPEGTQPG KQFRLKGKGM PVLRSAQTGD LYIQIQIETP QKLSKRQREL LQEFEQLSSK
ENNPESTGFF ARMKKFFDG
