ID   DNAK_DICNV              Reviewed;         642 AA.
AC   A5EYG3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-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=DNO_0826;
OS   Dichelobacter nodosus (strain VCS1703A).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cardiobacteriales;
OC   Cardiobacteriaceae; Dichelobacter.
OX   NCBI_TaxID=246195;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VCS1703A;
RX   PubMed=17468768; DOI=10.1038/nbt1302;
RA   Myers G.S.A., Parker D., Al-Hasani K., Kennan R.M., Seemann T., Ren Q.,
RA   Badger J.H., Selengut J.D., Deboy R.T., Tettelin H., Boyce J.D.,
RA   McCarl V.P., Han X., Nelson W.C., Madupu R., Mohamoud Y., Holley T.,
RA   Fedorova N., Khouri H., Bottomley S.P., Whittington R.J., Adler B.,
RA   Songer J.G., Rood J.I., Paulsen I.T.;
RT   "Genome sequence and identification of candidate vaccine antigens from the
RT   animal pathogen Dichelobacter nodosus.";
RL   Nat. Biotechnol. 25:569-575(2007).
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; CP000513; ABQ13697.1; -; Genomic_DNA.
DR   RefSeq; WP_012031149.1; NC_009446.1.
DR   AlphaFoldDB; A5EYG3; -.
DR   SMR; A5EYG3; -.
DR   STRING; 246195.DNO_0826; -.
DR   PRIDE; A5EYG3; -.
DR   EnsemblBacteria; ABQ13697; ABQ13697; DNO_0826.
DR   KEGG; dno:DNO_0826; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000000248; 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; 1.
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..642
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059551"
FT   REGION          602..642
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        603..617
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        618..642
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         198
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   642 AA;  69701 MW;  9FF4F6A2E70CC4A1 CRC64;
     MGKIIGIDLG TTNSCVAVMD GDSAKVIENS EGTRTTPSII AFSDGEVLVG QPAKRQAVTN
     PKNTLYAIKR LIGRRFDEKE VQKDINLVPY NIVKSDNGDA WVEIDGKKMA PPEISARILQ
     KMKKTVEDYL GETITEAVIT VPAYFNDSQR QATKDAGRIA GLEVKRIINE PTAAALAYGI
     DRGAKDAKIA VYDLGGGTFD ISIIETIDLD EEGQQFEVLA TNGDTFLGGE DFDRRIIDYL
     VNEFKKEQGI DLTSDSLALQ RLKEAAEKAK IELSSSQQTD INLPYITADA SGPKHMNLKL
     TRAKLESLVA DLIERSLEPC RIAMKDAGLS NSDITDVILV GGQTRMPKVQ EAVKNFFGKE
     PRKDVNPDEA VAMGAAIQGG VLGGQVKDVL LLDVTPLSLG IETLGGVMTK LIEKNTTIPT
     KASQIFSTAE DNQSAVTIHI LQGERQQASA NKSLGRFDLS DIPPAPRGMP QIEVSFDIDA
     NGILNVSAKD KQTGKEQSII IKASSGLSDE EVARMVKDAE AHAEEDRKFQ ERIETKNSAE
     SMINGVEKAI SELGDEVTSD EKEKTEAAIK ALREVMKGED SDAIKEKTNA LMEAASSIMQ
     KAYAKMTEKQ QSDDGAGTQN ADHKEDDVVD ADFEEVKSDK KD