ID   DNAK_ALKMQ              Reviewed;         614 AA.
AC   A6TSM0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=Amet_3048;
OS   Alkaliphilus metalliredigens (strain QYMF).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Alkaliphilus.
OX   NCBI_TaxID=293826;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QYMF;
RX   PubMed=27811105; DOI=10.1128/genomea.01226-16;
RA   Hwang C., 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   Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F.,
RA   Land M.L., Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J.,
RA   Richardson P., Fields M.W.;
RT   "Complete genome sequence of Alkaliphilus metalliredigens strain QYMF, an
RT   alkaliphilic and metal-reducing bacterium isolated from borax-contaminated
RT   leachate ponds.";
RL   Genome Announc. 4:0-0(2016).
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; CP000724; ABR49188.1; -; Genomic_DNA.
DR   RefSeq; WP_012064154.1; NC_009633.1.
DR   AlphaFoldDB; A6TSM0; -.
DR   SMR; A6TSM0; -.
DR   STRING; 293826.Amet_3048; -.
DR   PRIDE; A6TSM0; -.
DR   EnsemblBacteria; ABR49188; ABR49188; Amet_3048.
DR   KEGG; amt:Amet_3048; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_9; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000001572; 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..614
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059504"
FT   REGION          579..614
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        590..614
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         175
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   614 AA;  66493 MW;  F7E756C0F32B80D6 CRC64;
     MGKVIGIDLG TTNSCVAVLE GGEPVVIPNS EGNRTTPSVV AFGKDGERIV GEPAKRQAVV
     NPEKTIISIK THMGSDHKVA IDDKNYTPED ISAMILQKIK ADAEAYLGEA VTDAVITVPA
     YFTDSQRQAT KDAGKIAGLN VRRIINEPTA ASLAYGLDKT DEHQKILVYD LGGGTFDVSI
     LELGDGVFEV LATNGNNNLG GDDFDQALMD YIAEAFKKQE GIDLRKDKMS LQRLKEASEK
     AKQELSSTMT SSINLPFITA TNEGPKHLNM DITRSKFDEI TSHLVEKTMG PMRSALKDAG
     LSASDINKII LVGGSTRIPA VQQAVKKITN QDPHKGVNPD ECVAVGAAIQ AGVLTGEVKD
     VLLLDVTPLS LGIETLGGVF TRLIERNTTI PSKKSQTFST AADNQPAVDI HVLQGEREMA
     AGNVSLGRFE LSGIPPAHRG IPQIEVTFDI DANGIVNVSA KDLGTGKEQK ITITASTKLS
     DEEIEKKIKE AEEHAEEDKM QKEKIEVRNQ ADSLVYQIEK TLKESEGKID KEEEGKVTAE
     LEKLKKAVES DIVEDMKKAI EDVNTVFHAI SQKLYEQAAQ AQEAEGQEQA GDDNIVDAEY
     EEVKDEETQG EDEK