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 03-AUG-2022, entry version 154.
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}.
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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 AlphaFoldDB; P17631; -.
DR SMR; P17631; -.
DR IntAct; P17631; 2.
DR STRING; 224308.BSU25460; -.
DR jPOST; P17631; -.
DR PRIDE; P17631; -.
DR EnsemblBacteria; CAB14488; CAB14488; BSU_25460.
DR GeneID; 937848; -.
DR KEGG; bsu:BSU25460; -.
DR PATRIC; fig|224308.179.peg.2767; -.
DR eggNOG; COG0484; Bacteria.
DR InParanoid; P17631; -.
DR OMA; DLHCTVT; -.
DR PhylomeDB; P17631; -.
DR BioCyc; BSUB:BSU25460-MON; -.
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;
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 BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 202
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="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
