DNAJ_BRUO2
ID DNAJ_BRUO2 Reviewed; 377 AA.
AC Q05980; A5VT78;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Chaperone protein DnaJ {ECO:0000255|HAMAP-Rule:MF_01152};
GN Name=dnaJ {ECO:0000255|HAMAP-Rule:MF_01152}; OrderedLocusNames=BOV_2042;
OS Brucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=444178;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1459952; DOI=10.1128/jb.174.24.8036-8042.1992;
RA Cellier M.F.M., Teyssier J., Nicolas M., Liautard J.P., Marti J.,
RA Sri Widada J.;
RT "Cloning and characterization of the Brucella ovis heat shock protein DnaK
RT functionally expressed in Escherichia coli.";
RL J. Bacteriol. 174:8036-8042(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25840 / 63/290 / NCTC 10512;
RX PubMed=19436743; DOI=10.1371/journal.pone.0005519;
RA Tsolis R.M., Seshadri R., Santos R.L., Sangari F.J., Lobo J.M.,
RA de Jong M.F., Ren Q., Myers G., Brinkac L.M., Nelson W.C., Deboy R.T.,
RA Angiuoli S., Khouri H., Dimitrov G., Robinson J.R., Mulligan S.,
RA Walker R.L., Elzer P.E., Hassan K.A., Paulsen I.T.;
RT "Genome degradation in Brucella ovis corresponds with narrowing of its host
RT range and tissue tropism.";
RL PLoS ONE 4:E5519-E5519(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 -!- INDUCTION: By heat shock.
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; M95799; AAC36133.1; -; Genomic_DNA.
DR EMBL; CP000708; ABQ61985.1; -; Genomic_DNA.
DR PIR; B47042; B47042.
DR RefSeq; WP_006014538.1; NC_009505.1.
DR AlphaFoldDB; Q05980; -.
DR SMR; Q05980; -.
DR EnsemblBacteria; ABQ61985; ABQ61985; BOV_2042.
DR GeneID; 45125374; -.
DR KEGG; bov:BOV_2042; -.
DR HOGENOM; CLU_017633_0_7_5; -.
DR OMA; DLHCTVT; -.
DR PhylomeDB; Q05980; -.
DR PRO; PR:Q05980; -.
DR Proteomes; UP000006383; Chromosome I.
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 2: Evidence at transcript level;
KW Chaperone; Cytoplasm; DNA replication; Metal-binding; Repeat;
KW Stress response; Zinc; Zinc-finger.
FT CHAIN 1..377
FT /note="Chaperone protein DnaJ"
FT /id="PRO_0000070743"
FT DOMAIN 4..69
FT /note="J"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT REPEAT 148..155
FT /note="CXXCXGXG motif"
FT REPEAT 165..172
FT /note="CXXCXGXG motif"
FT REPEAT 187..194
FT /note="CXXCXGXG motif"
FT REPEAT 201..208
FT /note="CXXCXGXG motif"
FT ZN_FING 135..213
FT /note="CR-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 190
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT CONFLICT 87
FT /note="G -> A (in Ref. 1; AAC36133)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="G -> R (in Ref. 1; AAC36133)"
FT /evidence="ECO:0000305"
FT CONFLICT 111..115
FT /note="SNGGR -> NGA (in Ref. 1; AAC36133)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="V -> C (in Ref. 1; AAC36133)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="E -> K (in Ref. 1; AAC36133)"
FT /evidence="ECO:0000305"
FT CONFLICT 211..213
FT /note="TQE -> DRG (in Ref. 1; AAC36133)"
FT /evidence="ECO:0000305"
FT CONFLICT 223..228
FT /note="GIEDGT -> VSRTEP (in Ref. 1; AAC36133)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="F -> L (in Ref. 1; AAC36133)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="V -> G (in Ref. 1; AAC36133)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 377 AA; 41143 MW; B62EA1F1660E4572 CRC64;
MKIDYYEALG VTRTADDKTL KAAFRKLAMQ YHPDRNPDDP EAERKFKEIG EAYETLKDPQ
KRAAYDRFGH AAFENGGMGG GFGNGFGGAG GFADIFEDIF GEMMGGGRRR SNGGRERGAD
LRYNMEVTLE EAYAGKTAQI RVPTSITCDE CSGSGAKPGS QPTTCTMCSG SGRVRAAQGF
FSVERTCPGC NGRGQIIKDP CEKCHGQGRV TQERSLSVNI PAGIEDGTRI RLAGEGEAGL
RGGPAGDLYI FLSVKPHEFF QRDGADLYCK VPISMTTAAL GGQFEVSTLD GTQTRVKVPE
GTQNGKQFRL KGKGMPVLRQ SVTGDLYIQI DIETPQNLSK RQRELLEEFE KLSWQENSPK
SAGLFSRMKE FFEGIGE
