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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
 
 
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