ID   DNAK_ACICJ              Reviewed;         635 AA.
AC   A5FZ19;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=Acry_1646;
OS   Acidiphilium cryptum (strain JF-5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acidiphilium.
OX   NCBI_TaxID=349163;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JF-5;
RG   US DOE Joint Genome Institute;
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   Sims D., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P.;
RT   "Complete sequence of chromosome of Acidiphilium cryptum JF-5.";
RL   Submitted (MAY-2007) 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; CP000697; ABQ30851.1; -; Genomic_DNA.
DR   RefSeq; WP_007421611.1; NC_009484.1.
DR   AlphaFoldDB; A5FZ19; -.
DR   SMR; A5FZ19; -.
DR   STRING; 349163.Acry_1646; -.
DR   PRIDE; A5FZ19; -.
DR   EnsemblBacteria; ABQ30851; ABQ30851; Acry_1646.
DR   KEGG; acr:Acry_1646; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_5; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000000245; 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..635
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059498"
FT   REGION          601..635
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        619..635
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   635 AA;  68025 MW;  78719C8D2E5D6445 CRC64;
     MSKVIGIDLG TTNSCVAIME GKDVRVIENS EGARTTPSMV AFSESNERLV GQSAKRQAVT
     NPTNTLYAVK RLIGRRYDDP TVEKDKGLVS YNIVRGDNGD AWVESRGQRY APSQISSFVL
     TKMKETAEAY LGEAVTQAVI TVPAYFNDAQ RQATKDAGKI AGLEVLRIIN EPTAAALAYG
     MDKKQGGTIA VYDLGGGTFD ISILELGDGV FEVKSTNGDT FLGGEDFDQR VIDYLAEEFK
     REQGIDLRKD KLALQRLKEA AEKAKIELSS SKETEINLPF ITADASGPKH LVMKLTRAKL
     ESLVDDLVER TLGPCRAALK DAGVTAGEID EVILVGGMTR MPKVIETVKT FFGKEPARNV
     NPDEVVAIGA AIQGAVLKGD VKDVLLLDVT PLSLGIETLG GVFTRLIDRN TTIPTKKSQT
     FSTADDNQTA VTIKVYQGER EMAADNKLLG NFDLTGIPPA PRGVPQIEVT FDIDANGIVS
     VSAKDKATGK EQQIRIQASG GLSDTDIERM VKDAEANAAA DKAKRELVDA RNHADGLVHQ
     TEKTLKDNEG KVSAQDKGEA EAAIAAVRSA LEGSDLEAIK SATERLTQVA MRIGEAMYKA
     QAEAGAAQPG AETAAPGDKV VDAEFEDVDD KKKSA