DNAK_NOCSJ
ID DNAK_NOCSJ Reviewed; 621 AA.
AC A1SPX5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Chaperone protein DnaK {ECO:0000255|HAMAP-Rule:MF_00332};
DE AltName: Full=HSP70 {ECO:0000255|HAMAP-Rule:MF_00332};
DE AltName: Full=Heat shock 70 kDa protein {ECO:0000255|HAMAP-Rule:MF_00332};
DE AltName: Full=Heat shock protein 70 {ECO:0000255|HAMAP-Rule:MF_00332};
GN Name=dnaK {ECO:0000255|HAMAP-Rule:MF_00332}; OrderedLocusNames=Noca_4363;
OS Nocardioides sp. (strain ATCC BAA-499 / JS614).
OC Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae;
OC Nocardioides.
OX NCBI_TaxID=196162;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-499 / JS614;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Mattes T., Gossett J.,
RA Richardson P.;
RT "Complete sequence of chromosome 1 of Nocardioides sp. JS614.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a chaperone. {ECO:0000255|HAMAP-Rule:MF_00332}.
CC -!- INDUCTION: By stress conditions e.g. heat shock. {ECO:0000255|HAMAP-
CC Rule:MF_00332}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000255|HAMAP-Rule:MF_00332}.
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DR EMBL; CP000509; ABL83860.1; -; Genomic_DNA.
DR RefSeq; WP_011757789.1; NC_008699.1.
DR AlphaFoldDB; A1SPX5; -.
DR SMR; A1SPX5; -.
DR STRING; 196162.Noca_4363; -.
DR PRIDE; A1SPX5; -.
DR EnsemblBacteria; ABL83860; ABL83860; Noca_4363.
DR KEGG; nca:Noca_4363; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_11; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000000640; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR HAMAP; MF_00332; DnaK; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR012725; Chaperone_DnaK.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR19375; PTHR19375; 2.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR02350; prok_dnaK; 1.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Stress response.
FT CHAIN 1..621
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000059620"
FT REGION 580..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..613
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 174
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 621 AA; 66109 MW; F6AC9C0B0E066F4D CRC64;
MARAVGIDLG TTNSVVAVLE GGEPTVIANA EGARTTPSVV AFAKSGEVLV GEVAKRQAVT
NVDRTIRSVK RHMGTDWLTK IDDKDFTPQQ ISAFVLQKLK RDAEAYLGEP VTDAVITVPA
YFSDAQRQAT KEAGEIAGLN VSRIVNEPTA AALAYGLDKG DDQTILVFDL GGGTFDVSLL
EIGEGVVEVK ATSGDNHLGG DDWDARIVDW MVKKFKDNNG VDLAADKIAK QRLQEAAEKA
KIELSSSSET TIHLPYITHG ESGPLHFEEK LTRSEFQRLT TDLLDRTKGP FQSVLKDGGV
AIKDIDHVVL VGGSTRMPAV TEVVKELLGG KEPNKGVNPD EVVAVGAALQ AGVLKGEVKD
VLLLDVTPLS LGIETKGGVM TTLIERNTTI PTKRSEIFTT ADDNQPSVEI KVAQGERQMW
AQNQPLGNFE LTGLPPAPRG IPKIEVTFDI DANGIVHVTA KDQASGKEQS MTISGGSALG
KDEIDRMVRE AEQYAEEDAK RREAVETRNQ AEQLVYTTEK FLDENSDKLP DDVKTEVRAD
VDALKVTLEK EDASADDIRA GVTKLGESSQ KMGAAMYAAA EADSAAAGGS AGATGESDDD
VVDAEIVDEG GADDGAEGES K