(data stored in SCRATCH zone)

SWISSPROT: DNAJ_BACSU

ID   DNAJ_BACSU              Reviewed;         375 AA.
AC   P17631;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 3.
DT   11-DEC-2019, entry version 146.
DE   RecName: Full=Chaperone protein DnaJ {ECO:0000255|HAMAP-Rule:MF_01152};
GN   Name=dnaJ {ECO:0000255|HAMAP-Rule:MF_01152}; OrderedLocusNames=BSU25460;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / MB11;
RX   PubMed=1339421; DOI=10.1128/jb.174.10.3300-3310.1992;
RA   Wetzstein M., Voelker U., Dedio J., Loebau S., Zuber U., Schiesswohl M.,
RA   Herget C., Hecker M., Schumann W.;
RT   "Cloning, sequencing, and molecular analysis of the dnaK locus from
RT   Bacillus subtilis.";
RL   J. Bacteriol. 174:3300-3310(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   SEQUENCE REVISION TO 110-114; 245-247 AND 296-297.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24.
RC   STRAIN=168 / MB11;
RX   PubMed=2110662; DOI=10.1093/nar/18.8.2172;
RA   Wetzstein M., Schumann W.;
RT   "Complete nucleotide sequence of the Bacillus subtilis dnaK gene.";
RL   Nucleic Acids Res. 18:2172-2172(1990).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 257-372.
RC   STRAIN=168 / JH642;
RX   PubMed=9023197; DOI=10.1128/jb.179.4.1153-1164.1997;
RA   Homuth G., Masuda S., Mogk A., Kobayashi Y., Schumann W.;
RT   "The dnaK operon of Bacillus subtilis is heptacistronic.";
RL   J. Bacteriol. 179:1153-1164(1997).
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}.
DR   EMBL; M84964; AAA22529.1; -; Genomic_DNA.
DR   EMBL; D84432; BAA12465.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14488.2; -; Genomic_DNA.
DR   EMBL; X52064; CAA36287.1; -; Genomic_DNA.
DR   EMBL; D83717; BAA12077.1; -; Genomic_DNA.
DR   PIR; B41874; B41874.
DR   RefSeq; NP_390424.2; NC_000964.3.
DR   RefSeq; WP_003230010.1; NZ_JNCM01000036.1.
DR   SMR; P17631; -.
DR   IntAct; P17631; 2.
DR   STRING; 224308.BSU25460; -.
DR   jPOST; P17631; -.
DR   PRIDE; P17631; -.
DR   EnsemblBacteria; CAB14488; CAB14488; BSU25460.
DR   GeneID; 937848; -.
DR   KEGG; bsu:BSU25460; -.
DR   PATRIC; fig|224308.179.peg.2767; -.
DR   HOGENOM; HOG000226717; -.
DR   InParanoid; P17631; -.
DR   KO; K03686; -.
DR   OMA; MNMDDIF; -.
DR   PhylomeDB; P17631; -.
DR   BioCyc; BSUB:BSU25460-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0042026; P:protein refolding; IBA:GO_Central.
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;
DR   PRODOM; P17631.
DR   SWISS-2DPAGE; P17631.
KW   Chaperone; Cytoplasm; DNA replication; Metal-binding; Reference proteome;
KW   Repeat; Stress response; Zinc; Zinc-finger.
FT   CHAIN           1..375
FT                   /note="Chaperone protein DnaJ"
FT                   /id="PRO_0000070727"
FT   DOMAIN          5..69
FT                   /note="J"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT   REPEAT          145..152
FT                   /note="CXXCXGXG motif"
FT   REPEAT          162..169
FT                   /note="CXXCXGXG motif"
FT   REPEAT          188..195
FT                   /note="CXXCXGXG motif"
FT   REPEAT          202..209
FT                   /note="CXXCXGXG motif"
FT   ZN_FING         132..214
FT                   /note="CR-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT   COMPBIAS        76..103
FT                   /note="Gly-rich"
FT   METAL           145
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT   METAL           148
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT   METAL           162
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT   METAL           165
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT   METAL           188
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT   METAL           191
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT   METAL           202
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT   METAL           205
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT   CONFLICT        110..114
FT                   /note="NAPRQ -> KLRAR (in Ref. 1; AAA22529 and 2;
FT                   BAA12465)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        245..247
FT                   /note="PAG -> LP (in Ref. 1; AAA22529 and 2; BAA12465)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        296..297
FT                   /note="Missing (in Ref. 1; AAA22529, 2; BAA12465 and 6;
FT                   BAA12077)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   375 AA;  41045 MW;  F9A06A468E7B1643 CRC64;
     MSKRDYYEVL GVSKSASKDE IKKAYRKLSK KYHPDINKEA GSDEKFKEVK EAYETLSDDQ
     KRAHYDQFGH TDPNQGFGGG GFGGGDFGGF GFDDIFSSIF GGGTRRRDPN APRQGADLQY
     TMTLSFEDAA FGKETTIEIP REETCETCKG SGAKPGTNPE TCSHCGGSGQ LNVEQNTPFG
     KVVNRRVCHH CEGTGKIIKN KCADCGGKGK IKKRKKINVT IPAGVDDGQQ LRLSGQGEPG
     INGGPAGDLF VVFHVRAHEF FERDGDDIYC EMPLTFAQAA LGDEVEVPTL HGKVKLKIPA
     GTQTGTKFRL RGKGVQNVRG YGQGDQHIVV RVVTPTNLTD KQKDIIREFA EVSGNLPDEQ
     EMSFFDKVKR AFKGD
//

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