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ID A8LDT3_FRASN Unreviewed; 393 AA.
AC A8LDT3;
DT 04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT 04-DEC-2007, sequence version 1.
DT 08-MAY-2019, entry version 83.
DE RecName: Full=Chaperone protein DnaJ {ECO:0000256|HAMAP-Rule:MF_01152};
GN Name=dnaJ {ECO:0000256|HAMAP-Rule:MF_01152};
GN OrderedLocusNames=Franean1_0231 {ECO:0000313|EMBL:ABW09698.1};
OS Frankia sp. (strain EAN1pec).
OC Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=298653 {ECO:0000313|EMBL:ABW09698.1, ECO:0000313|Proteomes:UP000001313};
RN [1] {ECO:0000313|Proteomes:UP000001313}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EAN1pec {ECO:0000313|Proteomes:UP000001313};
RX PubMed=17151343; DOI=10.1101/gr.5798407;
RA Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N.,
RA Couloux A., Cournoyer B., Cruveiller S., Daubin V., Demange N.,
RA Francino M.P., Goltsman E., Huang Y., Kopp O.R., Labarre L.,
RA Lapidus A., Lavire C., Marechal J., Martinez M., Mastronunzio J.E.,
RA Mullin B.C., Niemann J., Pujic P., Rawnsley T., Rouy Z.,
RA Schenowitz C., Sellstedt A., Tavares F., Tomkins J.P., Vallenet D.,
RA Valverde C., Wall L.G., Wang Y., Medigue C., Benson D.R.;
RT "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT reflect host range and host plant biogeography.";
RL Genome Res. 17:7-15(2007).
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; CP000820; ABW09698.1; -; Genomic_DNA.
DR RefSeq; WP_012157675.1; NC_009921.1.
DR STRING; 298653.Franean1_0231; -.
DR EnsemblBacteria; ABW09698; ABW09698; Franean1_0231.
DR KEGG; fre:Franean1_0231; -.
DR eggNOG; ENOG4105BZ5; Bacteria.
DR eggNOG; COG0484; LUCA.
DR HOGENOM; HOG000226717; -.
DR KO; K03686; -.
DR OMA; MKIKRKT; -.
DR OrthoDB; 1738789at2; -.
DR BioCyc; FSP298653:G1G9X-223-MONOMER; -.
DR Proteomes; UP000001313; 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; A8LDT3.
DR SWISS-2DPAGE; A8LDT3.
KW Chaperone {ECO:0000256|HAMAP-Rule:MF_01152,
KW ECO:0000256|SAAS:SAAS00880482};
KW Complete proteome {ECO:0000313|Proteomes:UP000001313};
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:UP000001313};
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 160 238 CR-type. {ECO:0000259|PROSITE:PS51188}.
FT REPEAT 173 180 CXXCXGXG motif. {ECO:0000256|HAMAP-Rule:
FT MF_01152}.
FT REPEAT 190 197 CXXCXGXG motif. {ECO:0000256|HAMAP-Rule:
FT MF_01152}.
FT REPEAT 212 219 CXXCXGXG motif. {ECO:0000256|HAMAP-Rule:
FT MF_01152}.
FT REPEAT 226 233 CXXCXGXG motif. {ECO:0000256|HAMAP-Rule:
FT MF_01152}.
FT ZN_FING 160 238 CR-type. {ECO:0000256|PROSITE-ProRule:
FT PRU00546}.
FT METAL 173 173 Zinc 1. {ECO:0000256|HAMAP-Rule:
FT MF_01152}.
FT METAL 176 176 Zinc 1. {ECO:0000256|HAMAP-Rule:
FT MF_01152}.
FT METAL 190 190 Zinc 2. {ECO:0000256|HAMAP-Rule:
FT MF_01152}.
FT METAL 193 193 Zinc 2. {ECO:0000256|HAMAP-Rule:
FT MF_01152}.
FT METAL 212 212 Zinc 2. {ECO:0000256|HAMAP-Rule:
FT MF_01152}.
FT METAL 215 215 Zinc 2. {ECO:0000256|HAMAP-Rule:
FT MF_01152}.
FT METAL 226 226 Zinc 1. {ECO:0000256|HAMAP-Rule:
FT MF_01152}.
FT METAL 229 229 Zinc 1. {ECO:0000256|HAMAP-Rule:
FT MF_01152}.
SQ SEQUENCE 393 AA; 41229 MW; E97D0FEF15CE77FB CRC64;
MSVRDMVEKD YYAALGVPKD ASAADIKKAY RKLARELHPD KNPGDVKAEA RFKEVSEAYD
VLSDENRRRE YDEARALFAS GSYPGAGGRG GGMGGFGTPG GYGPGAGNLN LDDLLNGNGG
GGLGGIFDNL FQRTPTGRAP RRGTDIAAEV TISFEKSLTG LEATVRLPGA ATCATCAGIG
ARPGTSPRTC PVCRGLGVIS RSQGGFALSE PCRDCLGKGS LIDHPCPDCH GTGRREREQR
IRIPAGVSDG QRLRVRGRGS PGERGGAAGD LEVTVHVQSH PVFGREGHNL TINLPVTITE
AALGASVKVP TIDGTPLTVK VPAGTSSGRR LRARNRGVPR PGGENGDLIV TLEVTVPKPS
ELSPKARTAL QEFARAHPED PRESLIAQME GRA
//
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