DNAJ1_MYCTU
ID DNAJ1_MYCTU Reviewed; 395 AA.
AC P9WNV9; A7BJ09; F2GN42; O08380; P07881; P0A548;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Chaperone protein DnaJ 1 {ECO:0000255|HAMAP-Rule:MF_01152};
GN Name=dnaJ1 {ECO:0000255|HAMAP-Rule:MF_01152}; OrderedLocusNames=Rv0352;
GN ORFNames=MTCY13E10.12;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX PubMed=3126487; DOI=10.1093/nar/16.4.1636;
RA Lathigra R.;
RT "A gene from Mycobacterium tuberculosis which is homologous to the DnaJ
RT heat shock protein of E. coli.";
RL Nucleic Acids Res. 16:1636-1636(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35801 / TMC 107 / Erdman;
RA Lathigra R., Alexander B., Stover C.K., Coadwell J., Young R.A.,
RA Young D.B.;
RL Submitted (FEB-1991) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=GTC 601;
RX PubMed=17640840; DOI=10.1016/j.syapm.2007.06.003;
RA Yamada-Noda M., Ohkusu K., Hata H., Shah M.M., Nhung P.H., Sun X.S.,
RA Hayashi M., Ezaki T.;
RT "Mycobacterium species identification - A new approach via dnaJ gene
RT sequencing.";
RL Syst. Appl. Microbiol. 30:453-462(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [5]
RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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 -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC -!- SIMILARITY: Belongs to the DnaJ family. {ECO:0000255|HAMAP-
CC Rule:MF_01152}.
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DR EMBL; X06422; CAA29731.1; -; Genomic_DNA.
DR EMBL; X58406; CAA41308.1; -; Genomic_DNA.
DR EMBL; AB292558; BAF74477.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP43082.1; -; Genomic_DNA.
DR PIR; A70575; A70575.
DR RefSeq; WP_003401821.1; NZ_NVQJ01000002.1.
DR RefSeq; YP_177719.1; NC_000962.3.
DR AlphaFoldDB; P9WNV9; -.
DR SMR; P9WNV9; -.
DR STRING; 83332.Rv0352; -.
DR PaxDb; P9WNV9; -.
DR DNASU; 886495; -.
DR GeneID; 45424318; -.
DR GeneID; 886495; -.
DR KEGG; mtu:Rv0352; -.
DR TubercuList; Rv0352; -.
DR eggNOG; COG0484; Bacteria.
DR OMA; RVCPTCV; -.
DR PhylomeDB; P9WNV9; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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:2000679; P:positive regulation of transcription regulatory region DNA binding; IDA:CAFA.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IDA:MTBBASE.
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 1: Evidence at protein level;
KW Chaperone; Cytoplasm; DNA replication; Metal-binding; Reference proteome;
KW Repeat; Stress response; Zinc; Zinc-finger.
FT CHAIN 1..395
FT /note="Chaperone protein DnaJ 1"
FT /id="PRO_0000070835"
FT DOMAIN 10..75
FT /note="J"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT REPEAT 177..184
FT /note="CXXCXGXG motif"
FT REPEAT 194..201
FT /note="CXXCXGXG motif"
FT REPEAT 216..223
FT /note="CXXCXGXG motif"
FT REPEAT 230..237
FT /note="CXXCXGXG motif"
FT ZN_FING 164..242
FT /note="CR-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 216
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 219
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 230
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT BINDING 233
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152"
FT CONFLICT 342..395
FT /note="GVPKRSGGSGDLLVTVKVAVPPNLAGAAQEALEAYAAAERSSGFNPRAGWAG
FT NR -> VCPSAVGVAATYLSP (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 395 AA; 41345 MW; E75B7B932BB6E9B1 CRC64;
MAQREWVEKD FYQELGVSSD ASPEEIKRAY RKLARDLHPD ANPGNPAAGE RFKAVSEAHN
VLSDPAKRKE YDETRRLFAG GGFGGRRFDS GFGGGFGGFG VGGDGAEFNL NDLFDAASRT
GGTTIGDLFG GLFGRGGSAR PSRPRRGNDL ETETELDFVE AAKGVAMPLR LTSPAPCTNC
HGSGARPGTS PKVCPTCNGS GVINRNQGAF GFSEPCTDCR GSGSIIEHPC EECKGTGVTT
RTRTINVRIP PGVEDGQRIR LAGQGEAGLR GAPSGDLYVT VHVRPDKIFG RDGDDLTVTV
PVSFTELALG STLSVPTLDG TVGVRVPKGT ADGRILRVRG RGVPKRSGGS GDLLVTVKVA
VPPNLAGAAQ EALEAYAAAE RSSGFNPRAG WAGNR
