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DNAJ_RUEPO
ID   DNAJ_RUEPO              Reviewed;         381 AA.
AC   Q5LWJ5;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Chaperone protein DnaJ {ECO:0000255|HAMAP-Rule:MF_01152};
GN   Name=dnaJ {ECO:0000255|HAMAP-Rule:MF_01152}; OrderedLocusNames=SPO0044;
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter
OS   pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.M.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M.,
RA   Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q.,
RA   Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA   Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine
RT   environment.";
RL   Nature 432:910-913(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
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   -!- 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; CP000031; AAV93375.1; -; Genomic_DNA.
DR   RefSeq; WP_011045816.1; NC_003911.12.
DR   AlphaFoldDB; Q5LWJ5; -.
DR   SMR; Q5LWJ5; -.
DR   STRING; 246200.SPO0044; -.
DR   PRIDE; Q5LWJ5; -.
DR   EnsemblBacteria; AAV93375; AAV93375; SPO0044.
DR   KEGG; sil:SPO0044; -.
DR   eggNOG; COG0484; Bacteria.
DR   HOGENOM; CLU_017633_0_7_5; -.
DR   OMA; DLHCTVT; -.
DR   OrthoDB; 1738789at2; -.
DR   Proteomes; UP000001023; 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;
KW   Chaperone; Cytoplasm; DNA replication; Metal-binding; Reference proteome;
KW   Repeat; Stress response; Zinc; Zinc-finger.
FT   CHAIN           1..381
FT                   /note="Chaperone protein DnaJ"
FT                   /id="PRO_0000070881"
FT   DOMAIN          5..70
FT                   /note="J"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT   REPEAT          153..160
FT                   /note="CXXCXGXG motif"
FT   REPEAT          170..177
FT                   /note="CXXCXGXG motif"
FT   REPEAT          192..199
FT                   /note="CXXCXGXG motif"
FT   REPEAT          206..213
FT                   /note="CXXCXGXG motif"
FT   ZN_FING         140..218
FT                   /note="CR-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT   BINDING         153
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT   BINDING         156
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT   BINDING         170
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT   BINDING         173
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT   BINDING         192
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT   BINDING         195
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT   BINDING         206
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT   BINDING         209
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
SQ   SEQUENCE   381 AA;  40662 MW;  7AF14809CDCCA456 CRC64;
     MSKRDYYDVL GVSKGASADE IKKAYRGKAK ELHPDRNKDN PDAESLFKEV NEAYEVLKDA
     EKKAAYDRFG HAAFEGGMGG GQRPGGGFGS GDFSSAFSDV FEDLFGDFMG GQRGGGGRRA
     ARGSDLRYNL RVTLEEAFSG LQKTINVPTA VACSSCEGTG AEGGVEPTTC PTCSGMGKVR
     AQQGFFTVER TCPTCSGLGQ IIKNPCKSCR GQGRVEKDRA LSVNIPAGVE TGTRIRLAGE
     GEAGMRGGPP GDLYIFVEVA KHELFERDGV NLYCRVPVSM AKAALGGAIE VPTIDGGRGR
     VQVPAGSQSG RQMRLRSKGM PALRGGGIGD MFIELAVETP VNLTSKQKDL LREFDELSED
     NNPETKSFFS SVKSFWDGMK G
 
 
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