ID A0A1N0PME2_9MYCO Unreviewed; 393 AA.
AC A0A1N0PME2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Chaperone protein DnaJ {ECO:0000256|HAMAP-Rule:MF_01152};
GN Name=dnaJ_2 {ECO:0000313|EMBL:SKR00246.1};
GN Synonyms=dnaJ {ECO:0000256|HAMAP-Rule:MF_01152}, dnaJ_1
GN {ECO:0000313|EMBL:SHY15005.1};
GN ORFNames=SAMEA2070793_00016 {ECO:0000313|EMBL:SHY15005.1},
GN SAMEA2071181_02420 {ECO:0000313|EMBL:SKR00246.1}, SAMEA2259684_05379
GN {ECO:0000313|EMBL:SHV27592.1};
OS Mycobacteroides abscessus subsp. abscessus.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacteroides; Mycobacteroides abscessus.
OX NCBI_TaxID=1185650 {ECO:0000313|EMBL:SKR00246.1, ECO:0000313|Proteomes:UP000190796};
RN [1] {ECO:0000313|Proteomes:UP000184807, ECO:0000313|Proteomes:UP000185014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22 {ECO:0000313|EMBL:SKR00246.1,
RC ECO:0000313|Proteomes:UP000190796}, 425 {ECO:0000313|EMBL:SHY15005.1,
RC ECO:0000313|Proteomes:UP000184807}, and 879
RC {ECO:0000313|EMBL:SHV27592.1, ECO:0000313|Proteomes:UP000185014};
RG Pathogen Informatics;
RL Submitted (NOV-2016) 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:0000256|HAMAP-Rule:MF_01152}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01152};
CC Note=Binds 2 Zn(2+) ions per monomer. {ECO:0000256|HAMAP-
CC Rule:MF_01152};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01152}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_01152}.
CC -!- SIMILARITY: Belongs to the DnaJ family. {ECO:0000256|HAMAP-
CC Rule:MF_01152}.
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DR EMBL; FSBZ01000592; SHV27592.1; -; Genomic_DNA.
DR EMBL; FSFZ01000001; SHY15005.1; -; Genomic_DNA.
DR EMBL; FVKR01000007; SKR00246.1; -; Genomic_DNA.
DR RefSeq; WP_005085701.1; NZ_SAZC01000002.1.
DR STRING; 36809.BAB79_23855; -.
DR GeneID; 66969706; -.
DR eggNOG; COG0484; Bacteria.
DR Proteomes; UP000184807; Unassembled WGS sequence.
DR Proteomes; UP000185014; Unassembled WGS sequence.
DR Proteomes; UP000190796; Unassembled WGS sequence.
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; cd10747; DnaJ_C; 1.
DR CDD; cd10719; DnaJ_zf; 1.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR Gene3D; 2.10.230.10; Heat shock protein DnaJ, cysteine-rich domain; 1.
DR Gene3D; 2.60.260.20; Urease metallochaperone UreE, N-terminal domain; 2.
DR HAMAP; MF_01152; DnaJ; 1.
DR InterPro; IPR012724; DnaJ.
DR InterPro; IPR002939; DnaJ_C.
DR InterPro; IPR001623; DnaJ_domain.
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 NCBIfam; TIGR02349; DnaJ_bact; 1.
DR PANTHER; PTHR43096:SF54; CHAPERONE PROTEIN DNAJ 1; 1.
DR PANTHER; PTHR43096; DNAJ HOMOLOG 1, MITOCHONDRIAL-RELATED; 1.
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; Chaperone J-domain; 1.
DR SUPFAM; SSF57938; DnaJ/Hsp40 cysteine-rich domain; 1.
DR SUPFAM; SSF49493; HSP40/DnaJ peptide-binding domain; 2.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51188; ZF_CR; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|HAMAP-Rule:MF_01152};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01152};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW Rule:MF_01152};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01152}; Reference proteome {ECO:0000313|Proteomes:UP000185014};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_01152};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_01152};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01152};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|HAMAP-
KW Rule:MF_01152}.
FT DOMAIN 10..75
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 162..240
FT /note="CR-type"
FT /evidence="ECO:0000259|PROSITE:PS51188"
FT REPEAT 175..182
FT /note="CXXCXGXG motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152"
FT REPEAT 192..199
FT /note="CXXCXGXG motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152"
FT REPEAT 214..221
FT /note="CXXCXGXG motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152"
FT REPEAT 228..235
FT /note="CXXCXGXG motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152"
FT ZN_FING 162..240
FT /note="CR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
FT REGION 35..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152"
FT BINDING 214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152"
FT BINDING 217
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152"
SQ SEQUENCE 393 AA; 41361 MW; EFB3F080E432DC52 CRC64;
MTQREWVEKD FYKELGVSST ATQDEIKKAA RKLLAENHPD RNPGNQAAED RYKAVSEAKD
VLSDPAKRKE YDETRRLFAG GGFGRRFGDN GFGGGGFSGG SNSAEFNLND LFGNADTSGG
GGIGDLFGGL FGQRAQPRAS RPRRGNDLET ETQLDFVEAC KGVSVPLRLT SPAPCTTCHG
SGARPGTSPK VCGSCNGSGV INRNQGAFGF SEPCADCRGT GSIIENPCTD CQGTGVTTRT
RTITVRIPPG VDDGQRIRLA GQGEAGLRGA PSGDLYVTVH VRPDKVFSRD GDDLTLTVPV
SFTELALGAT ISVPTLEGRV GVKVPAGTSD GRILRVRGRG IPKRAGGNGD LLVTVKVAVP
SKLEDSALEA LQRYQVAEKA SGFDPRAGWA GAR
//