(data stored in ACNUC10821 zone)

SWISSPROT: C8U190_ECO10

ID   C8U190_ECO10            Unreviewed;       376 AA.
AC   C8U190;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 69.
DE   RecName: Full=Chaperone protein DnaJ {ECO:0000256|HAMAP-Rule:MF_01152};
GN   Name=dnaJ {ECO:0000256|HAMAP-Rule:MF_01152,
GN   ECO:0000313|EMBL:BAI28898.1};
GN   OrderedLocusNames=ECO103_0015 {ECO:0000313|EMBL:BAI28898.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI28898.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI28898.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- FUNCTION: Participates actively in the response to hyperosmotic
CC       and heat shock by preventing the aggregation of stress-denatured
CC       proteins and by disaggregating proteins, also in an autonomous,
CC       DnaK-independent fashion. Unfolded proteins bind initially to
CC       DnaJ; upon interaction with the DnaJ-bound protein, DnaK
CC       hydrolyzes its bound ATP, resulting in the formation of a stable
CC       complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers
CC       the release of the substrate protein, thus completing the reaction
CC       cycle. Several rounds of ATP-dependent interactions between DnaJ,
CC       DnaK and GrpE are required for fully efficient folding. Also
CC       involved, together with DnaK and GrpE, in the DNA replication of
CC       plasmids through activation of initiation proteins.
CC       {ECO:0000256|HAMAP-Rule:MF_01152}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         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
CC       center 2 is essential for interaction with DnaK and for DnaJ
CC       activity. {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; AP010958; BAI28898.1; -; Genomic_DNA.
DR   RefSeq; WP_001118464.1; NC_013353.1.
DR   SMR; C8U190; -.
DR   EnsemblBacteria; BAI28898; BAI28898; ECO103_0015.
DR   KEGG; eoh:ECO103_0015; -.
DR   HOGENOM; HOG000226717; -.
DR   KO; K03686; -.
DR   OMA; DMGGFAD; -.
DR   BioCyc; ECOL585395:ECO103_RS00080-MONOMER; -.
DR   Proteomes; UP000000959; 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; 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;
DR   PRODOM; C8U190.
DR   SWISS-2DPAGE; C8U190.
KW   Chaperone {ECO:0000256|HAMAP-Rule:MF_01152,
KW   ECO:0000256|SAAS:SAAS00880482};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01152};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_01152};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01152, ECO:0000256|PROSITE-
KW   ProRule:PRU00546, ECO:0000256|SAAS:SAAS00880538};
KW   Repeat {ECO:0000256|HAMAP-Rule:MF_01152,
KW   ECO:0000256|SAAS:SAAS00880439};
KW   Stress response {ECO:0000256|HAMAP-Rule:MF_01152};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01152, ECO:0000256|PROSITE-
KW   ProRule:PRU00546, ECO:0000256|SAAS:SAAS00880462};
KW   Zinc-finger {ECO:0000256|HAMAP-Rule:MF_01152, ECO:0000256|PROSITE-
KW   ProRule:PRU00546, ECO:0000256|SAAS:SAAS00880536}.
FT   DOMAIN        5     70       J. {ECO:0000259|PROSITE:PS50076}.
FT   DOMAIN      131    209       CR-type. {ECO:0000259|PROSITE:PS51188}.
FT   REPEAT      144    151       CXXCXGXG motif. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   REPEAT      161    168       CXXCXGXG motif. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   REPEAT      183    190       CXXCXGXG motif. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   REPEAT      197    204       CXXCXGXG motif. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   ZN_FING     131    209       CR-type. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00546}.
FT   COMPBIAS     77    114       Gly-rich. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   METAL       144    144       Zinc 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   METAL       147    147       Zinc 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   METAL       161    161       Zinc 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   METAL       164    164       Zinc 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   METAL       183    183       Zinc 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   METAL       186    186       Zinc 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   METAL       197    197       Zinc 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
FT   METAL       200    200       Zinc 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01152}.
SQ   SEQUENCE   376 AA;  41044 MW;  8B7ADC315B7E6F4A CRC64;
     MAKQDYYEIL GVSKTAEERE IKKAYKRLAM KYHPDRNQGD KEAEAKFKEI KEAYEVLTDS
     QKRAAYDQYG HAAFEQGGMG GGGFGGGADF SDIFGDVFGD IFGGGRGRQR AARGADLRYN
     MELTLEEAVR GVTKEIRIPT LEECDVCHGS GAKPGTQPQT CPTCHGSGQV QMRQGFFAVQ
     QTCPHCQGRG TLIKDPCNKC HGHGRVERSK TLSVKIPAGV DTGDRIRLAG EGEAGEHGAP
     AGDLYVQVQV KQHPIFEREG NNLYCEVPIN FAMAALGGEI EVPTLDGRVK LKVPGETQTG
     KLFRMRGKGV KSVRGGAQGD LLCRVVVETP VGLNEKQKQL LQELQESFGG PTGEHNSPRS
     KSFFDGVKKF FDDLTR
//

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