DNAJ1_MYCLE
ID DNAJ1_MYCLE Reviewed; 388 AA.
AC Q02605;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Chaperone protein DnaJ 1 {ECO:0000255|HAMAP-Rule:MF_01152};
GN Name=dnaJ1 {ECO:0000255|HAMAP-Rule:MF_01152}; OrderedLocusNames=ML2494;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2051024;
RA McKenzie K.R., Adams E., Britton W.J., Garsia R.J., Basten A.;
RT "Sequence and immunogenicity of the 70-kDa heat shock protein of
RT Mycobacterium leprae.";
RL J. Immunol. 147:312-319(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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; M95576; AAA25363.1; -; Genomic_DNA.
DR EMBL; AL583925; CAC32011.1; -; Genomic_DNA.
DR PIR; C87221; C87221.
DR RefSeq; NP_302611.1; NC_002677.1.
DR RefSeq; WP_010908930.1; NC_002677.1.
DR AlphaFoldDB; Q02605; -.
DR SMR; Q02605; -.
DR STRING; 272631.ML2494; -.
DR EnsemblBacteria; CAC32011; CAC32011; CAC32011.
DR KEGG; mle:ML2494; -.
DR PATRIC; fig|272631.5.peg.4789; -.
DR Leproma; ML2494; -.
DR eggNOG; COG0484; Bacteria.
DR HOGENOM; CLU_017633_0_6_11; -.
DR OMA; RVCPTCV; -.
DR Proteomes; UP000000806; 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..388
FT /note="Chaperone protein DnaJ 1"
FT /id="PRO_0000070826"
FT DOMAIN 10..74
FT /note="J"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT REPEAT 172..179
FT /note="CXXCXGXG motif"
FT REPEAT 189..196
FT /note="CXXCXGXG motif"
FT REPEAT 211..218
FT /note="CXXCXGXG motif"
FT REPEAT 225..232
FT /note="CXXCXGXG motif"
FT ZN_FING 159..237
FT /note="CR-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 189
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 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 225
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT CONFLICT 27
FT /note="K -> N (in Ref. 1; AAA25363)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="A -> S (in Ref. 1; AAA25363)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="W -> C (in Ref. 1; AAA25363)"
FT /evidence="ECO:0000305"
FT CONFLICT 138..139
FT /note="RP -> S (in Ref. 1; AAA25363)"
FT /evidence="ECO:0000305"
FT CONFLICT 224..225
FT /note="PC -> LR (in Ref. 1; AAA25363)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="V -> A (in Ref. 1; AAA25363)"
FT /evidence="ECO:0000305"
FT CONFLICT 377..387
FT /note="SSGFNPRAGWG -> QVVSTLGRDGAGN (in Ref. 1; AAA25363)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 388 AA; 41307 MW; 0EBF0CF4E572A12C CRC64;
MAQREWVEKD FYKELGVSSD ASPEEIKRAY RKLARYLHPD ANPDNSAGER FKVVSEAHNV
LSDPVKRKEY DETRRLFAGG WLGGRRFDSS FGDFGMGGDG AEFNLNDLFD AASRTGGTNI
GDLFGGLFGR GASVRPSRPR RGNDLETEAD LDFVEAAKGV AMPLRLTSPA PCTNCHGSGA
RPGISPKVCS TCNGSGVINR NQGAFGFSEP CTECRGSGSI IEHPCEECKG TGVTTRTRTI
NVRIPSGVED GQRIRLAGQG EAGLRGAPSG DLYVTVHVRP DKIFGRNGDD LTVTIPVSFT
ELALGSTLSV PTLDGTVGVR VPKGTSDGRI LRVRGRGVPK RSGGHGDLLV TVKVAVPLNL
EGAAQKALEA YAAAERSSGF NPRAGWGR
