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ID E3J616_FRAIE Unreviewed; 391 AA.
AC E3J616;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 08-MAY-2019, entry version 57.
DE RecName: Full=Chaperone protein DnaJ {ECO:0000256|HAMAP-Rule:MF_01152};
GN Name=dnaJ {ECO:0000256|HAMAP-Rule:MF_01152};
GN OrderedLocusNames=FraEuI1c_0219 {ECO:0000313|EMBL:ADP78307.1};
OS Frankia inefficax (strain DSM 45817 / CECT 9037 / EuI1c).
OC Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=298654 {ECO:0000313|EMBL:ADP78307.1, ECO:0000313|Proteomes:UP000002484};
RN [1] {ECO:0000313|EMBL:ADP78307.1, ECO:0000313|Proteomes:UP000002484}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45817 / CECT 9037 / EuI1c
RC {ECO:0000313|Proteomes:UP000002484};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA Beauchemin N., Sen A., Sur S.A., Gtari M., Wall L., Tisa L., Woyke T.;
RT "Complete sequence of Frankia sp. EuI1c.";
RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01152}.
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DR EMBL; CP002299; ADP78307.1; -; Genomic_DNA.
DR RefSeq; WP_013421430.1; NC_014666.1.
DR STRING; 298654.FraEuI1c_0219; -.
DR EnsemblBacteria; ADP78307; ADP78307; FraEuI1c_0219.
DR KEGG; fri:FraEuI1c_0219; -.
DR eggNOG; ENOG4105BZ5; Bacteria.
DR eggNOG; COG0484; LUCA.
DR HOGENOM; HOG000226717; -.
DR KO; K03686; -.
DR OMA; MKIKRKT; -.
DR OrthoDB; 1738789at2; -.
DR BioCyc; FSP298654:G1GOT-222-MONOMER; -.
DR Proteomes; UP000002484; 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 PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51188; ZF_CR; 1.
PE 3: Inferred from homology;
DR PRODOM; E3J616.
DR SWISS-2DPAGE; E3J616.
KW Chaperone {ECO:0000256|HAMAP-Rule:MF_01152,
KW ECO:0000256|SAAS:SAAS00880482};
KW Complete proteome {ECO:0000313|Proteomes:UP000002484};
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 Reference proteome {ECO:0000313|Proteomes:UP000002484};
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 10 75 J. {ECO:0000259|PROSITE:PS50076}.
FT DOMAIN 159 237 CR-type. {ECO:0000259|PROSITE:PS51188}.
FT REPEAT 172 179 CXXCXGXG motif. {ECO:0000256|HAMAP-Rule:
FT MF_01152}.
FT REPEAT 189 196 CXXCXGXG motif. {ECO:0000256|HAMAP-Rule:
FT MF_01152}.
FT REPEAT 211 218 CXXCXGXG motif. {ECO:0000256|HAMAP-Rule:
FT MF_01152}.
FT REPEAT 225 232 CXXCXGXG motif. {ECO:0000256|HAMAP-Rule:
FT MF_01152}.
FT ZN_FING 159 237 CR-type. {ECO:0000256|PROSITE-ProRule:
FT PRU00546}.
FT METAL 172 172 Zinc 1. {ECO:0000256|HAMAP-Rule:
FT MF_01152}.
FT METAL 175 175 Zinc 1. {ECO:0000256|HAMAP-Rule:
FT MF_01152}.
FT METAL 189 189 Zinc 2. {ECO:0000256|HAMAP-Rule:
FT MF_01152}.
FT METAL 192 192 Zinc 2. {ECO:0000256|HAMAP-Rule:
FT MF_01152}.
FT METAL 211 211 Zinc 2. {ECO:0000256|HAMAP-Rule:
FT MF_01152}.
FT METAL 214 214 Zinc 2. {ECO:0000256|HAMAP-Rule:
FT MF_01152}.
FT METAL 225 225 Zinc 1. {ECO:0000256|HAMAP-Rule:
FT MF_01152}.
FT METAL 228 228 Zinc 1. {ECO:0000256|HAMAP-Rule:
FT MF_01152}.
SQ SEQUENCE 391 AA; 40858 MW; D0C0EBAE919F1B6D CRC64;
MSVRDMVEKD YYAALGVPKD APAADIKKAY RKLARELHPD KNPGDAKAEA RFKEVSEAYD
VLSDERRRRE YDEARALFQS GRFSGGPGGF PGNGGGYGSG YAGTGAGGGF GGSSGGINMD
DLLGGFGDLF QRQSPGRGPK RGVDIEAEVT ISFEKSLTGL EATVRIPGAA TCATCNGLGS
RPGTMPRTCP VCRGLGVISR SQGGFALSEP CRECLGKGQL IDHPCPDCHG SGRREREQRI
RIPAGVADGQ RLKVRGRGTP GERGGSPGDL EVTVHVQPHP VFGREGPNLT IALPITFSEA
TLGASVRVPT LDGAPLTVKV PPGTSSGKRL RAKGRGVPKT GGGNGDLIVT VEVAVPKPTD
LSPKARTALQ EFALAHPGDP REALMAQLGQ Q
//
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