DNAJ_LISM4
ID DNAJ_LISM4 Reviewed; 377 AA.
AC G2K045; Q9S5A3;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Chaperone protein DnaJ {ECO:0000255|HAMAP-Rule:MF_01152};
GN Name=dnaJ {ECO:0000255|HAMAP-Rule:MF_01152}; OrderedLocusNames=LMRG_00925;
OS Listeria monocytogenes serotype 1/2a (strain 10403S).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=393133;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=10403S;
RX PubMed=10701836; DOI=10.1379/1466-1268(2000)005<0021:csatao>2.0.co;2;
RA Hanawa T., Kai M., Kamiya S., Yamamoto T.;
RT "Cloning, sequencing, and transcriptional analysis of the dnaK heat shock
RT operon of Listeria monocytogenes.";
RL Cell Stress Chaperones 5:21-29(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10403S;
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Borowsky M., Borodovsky M., Young S.K., Zeng Q., Koehrsen M.,
RA Fitzgerald M., Wiedmann M., Swaminathan B., Lauer P., Portnoy D.,
RA Cossart P., Buchrieser C., Higgins D., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Borenstein D., Brown A., Chapman S.B., Chen Z.,
RA Dunbar C.D., Engels R., Freedman E., Gearin G., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heilman E., Heiman D., Howarth C., Jen D., Larson L.,
RA Lui A., MacDonald J., Mehta T., Montmayeur A., Neiman D., Park D.,
RA Pearson M., Priest M., Richards J., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA Haas B., Nusbaum C., Birren B.;
RT "The genome sequence of Listeria monocytogenes strain 10403S.";
RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
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; AB023064; BAA82790.1; -; Genomic_DNA.
DR EMBL; CP002002; AEO06457.1; -; Genomic_DNA.
DR PIR; T43739; T43739.
DR RefSeq; WP_010990134.1; NC_017544.1.
DR AlphaFoldDB; G2K045; -.
DR SMR; G2K045; -.
DR EnsemblBacteria; AEO06457; AEO06457; LMRG_00925.
DR KEGG; lmt:LMRG_00925; -.
DR HOGENOM; CLU_017633_0_7_9; -.
DR OMA; DLHCTVT; -.
DR Proteomes; UP000001288; 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; Repeat;
KW Stress response; Zinc; Zinc-finger.
FT CHAIN 1..377
FT /note="Chaperone protein DnaJ"
FT /id="PRO_0000418521"
FT DOMAIN 5..69
FT /note="J"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT REPEAT 147..154
FT /note="CXXCXGXG motif"
FT REPEAT 164..171
FT /note="CXXCXGXG motif"
FT REPEAT 190..197
FT /note="CXXCXGXG motif"
FT REPEAT 204..211
FT /note="CXXCXGXG motif"
FT ZN_FING 134..216
FT /note="CR-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 190
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
SQ SEQUENCE 377 AA; 41077 MW; 70A8C5836239310A CRC64;
MAKRDYYEVL GISKSASADE IKKAYRKLSK QYHPDINKEA GADEKFKEIS EAYEALSDPQ
KRAQYDQYGH VDPNQGFGGG GAGGGFGGGG FSGFEDIFDT FFGGGGRQQD PNAPRQGSDL
QYTMRLKFKE AIFGKDAEIE IPREENCDTC HGSGAKPGTT PEKCSHCGGK GSINVEQNTP
FGRVVNKRTC QYCNGTGKEI KEKCPTCHGK GRVTKTKKIK VKVPAGVNDG QQMRVSGEGE
AGINGGPNGD LYVVFVVIPD EFFEREADDI YVEVPITFVQ ATLGDEIDVP TVHGKVRLKI
PSGTQTGTTF RLRGKGVPHL RGNGTGDQHV IVKVIVPKKL DDKQKEILRE FASTTGDKVD
EQTSGFFDKM KRAFKGD
