ID Q0KKV6_STAAU Unreviewed; 296 AA.
AC Q0KKV6;
DT 03-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=DnaJ protein {ECO:0000313|EMBL:BAF30883.1};
DE Flags: Fragment;
GN Name=dnaJ {ECO:0000313|EMBL:BAF30883.1};
OS Staphylococcus aureus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280 {ECO:0000313|EMBL:BAF30883.1};
RN [1] {ECO:0000313|EMBL:BAF30883.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=GTC 286 {ECO:0000313|EMBL:BAF30883.1};
RA Shah M.M., Iihara H., Noda M., Song S.X., Nhung P.H., Ohkusu K.,
RA Kawamura Y., Ezaki T.;
RT "dnaJ gene sequence-based assay for species identification and phylogenetic
RT grouping in the genus Staphylococcus.";
RL Int. J. Syst. Evol. Microbiol. 57:25-30(2007).
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DR EMBL; AB234058; BAF30883.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0KKV6; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0031072; F:heat shock protein binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
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; 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 NCBIfam; TIGR02349; DnaJ_bact; 1.
DR PANTHER; PTHR43096:SF48; CHAPERONE PROTEIN DNAJ; 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; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51188; ZF_CR; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00546}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Stress response {ECO:0000256|ARBA:ARBA00023016};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00546};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00546}.
FT DOMAIN 1..61
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 128..210
FT /note="CR-type"
FT /evidence="ECO:0000259|PROSITE:PS51188"
FT ZN_FING 128..210
FT /note="CR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAF30883.1"
FT NON_TER 296
FT /evidence="ECO:0000313|EMBL:BAF30883.1"
SQ SEQUENCE 296 AA; 32026 MW; B3C3EB16C41B5B48 CRC64;
VLGISKDASK DEIKKAYRKL SKKYHPDINK EEGADEKFKE ISEAYEVLSD DNKRASYDQF
GHDGPQGFGG QGFNGSDFGG FSGFGGGGFE DIFSSFFGGG RQRDPNAPQK GDDLQYTMTL
TFEEAVFGTT KEISIRKDVT CETCHGDGAK PGTSKKTCSY CNGAGHVAVE QNTILGRVRT
EQVCPKCNGS GQEFEEACPT CHGKGTENKT VKLEVKVPEG VDNEQQIRLA GEGSPGVNGG
PAGDLYVVFR VKPSETFKRD GDDIYYKLNV SFPQAALGDE IKIPTLNNEV MLTIPA
//
