ID   DNAK_AROAE              Reviewed;         645 AA.
AC   Q5P1H5;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=AZOSEA27140;
GN   ORFNames=ebA4794;
OS   Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Aromatoleum.
OX   NCBI_TaxID=76114;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EbN1;
RX   PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA   Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA   Reinhardt R.;
RT   "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT   bacterium, strain EbN1.";
RL   Arch. Microbiol. 183:27-36(2005).
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; CR555306; CAI08839.1; -; Genomic_DNA.
DR   RefSeq; WP_011238522.1; NC_006513.1.
DR   AlphaFoldDB; Q5P1H5; -.
DR   SMR; Q5P1H5; -.
DR   STRING; 76114.ebA4794; -.
DR   EnsemblBacteria; CAI08839; CAI08839; ebA4794.
DR   KEGG; eba:ebA4794; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_4; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000006552; 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..645
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000225930"
FT   REGION          601..645
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         199
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   645 AA;  69452 MW;  2184F8856A04E48F CRC64;
     MGKIIGIDLG TTNSCVAVME GGKPKVIENS EGARTTPSVV AYAEDGEILT GAPAKRQAVT
     NAKNTLFAVK RLIGRRFEEK EVQKDIDLMP YTICKADNSD AWVEVRGKKI APPQVSAEVL
     RKMKKTAEDY LGEEVTEAVI TVPAYFNDSQ RQATKDAGRI AGLEVKRIIN EPTAAALAFG
     MDKKPGDSKI AVYDLGGGTF DISIIEIADI DGEHQFEVLA TNGDTFLGGE DFDQRLIDYI
     VTEFKKEQGV DLKKDVLALQ RLKEAAEKAK IELSSGQQTE VNLPYITADA SGPKHLAVKI
     TRAKFESLVE DLVQRTIEPC RVALKDAGLK INDIDDVILV GGQSRMPKVQ EKVKEFFGKE
     ARRDVNPDEA VAVGAAIQGG VLQGEVKDVL LLDVTPLSLG IETLGGVMTK LIQKNTTVPT
     KASQVFSTAD DNQSAVTIHV LQGEREMASG NKSLGQFNLS DIPPAPRGMP QIEVTFDIDA
     NGILHVSAKD KATGKENKIK IQANSGLSED EIQRMVQDAA AHAEEDKKAH ELVDIRNQCD
     ALVHSVKKSL TEYGDKISAD EKEKIEQAMK DAEEALKGND KDTIEARMQA LATASQKLGE
     QMYAQSQGAE GGATDEAAGG GSTGGSKAAD ADVVDAEFTE VKDKK