ID   DNAK1_THEVB             Reviewed;         651 AA.
AC   Q8DKR6;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Chaperone protein dnaK1;
DE   AltName: Full=HSP70-1;
DE   AltName: Full=Heat shock 70 kDa protein 1;
DE   AltName: Full=Heat shock protein 70-1;
GN   Name=dnaK1; OrderedLocusNames=tll0791;
OS   Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC   Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC   Thermosynechococcus.
OX   NCBI_TaxID=197221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX   PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA   Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA   Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA   Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takeuchi C., Yamada M., Tabata S.;
RT   "Complete genome structure of the thermophilic cyanobacterium
RT   Thermosynechococcus elongatus BP-1.";
RL   DNA Res. 9:123-130(2002).
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC   -!- INDUCTION: By stress conditions e.g. heat shock (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; BA000039; BAC08342.1; -; Genomic_DNA.
DR   RefSeq; NP_681580.1; NC_004113.1.
DR   RefSeq; WP_011056634.1; NC_004113.1.
DR   AlphaFoldDB; Q8DKR6; -.
DR   SMR; Q8DKR6; -.
DR   STRING; 197221.22294512; -.
DR   EnsemblBacteria; BAC08342; BAC08342; BAC08342.
DR   KEGG; tel:tll0791; -.
DR   PATRIC; fig|197221.4.peg.830; -.
DR   eggNOG; COG0443; Bacteria.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000000440; 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; 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..651
FT                   /note="Chaperone protein dnaK1"
FT                   /id="PRO_0000078560"
FT   MOD_RES         197
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   651 AA;  70377 MW;  43DF23CE801E561D CRC64;
     MGKIIGIDLG TTNSCVAVLE GGNPVVIPNA EGGRTTPSIV AFGKSGERLV GQLAKRQAIT
     NAENTIFSIK RFIGRRWEET AQERARVPYA CVPGRDGMVD VQIRDRTYTP QEISAMVLQK
     LKQDAEAYLG EPVTQAVITV PAYFSDAQRQ ATKDAGAIAG LEVLRIINEP TAASLAYGID
     KQDQDQTILV FDLGGGTFDV SILQLGDGVF EVRSTAGNNH LGGDNFDECI VDWLLACFKE
     QEGIDLSKDK MALQRLREAA EKAKVELSGT LSTSINLPFI TADETGPKHL EMELTRSKFE
     ELCAHLVQAT LEPMQQAIAD AGLTVEEIDR VLLVGGSTRI PAIQELVKQF CGKNPDRSVN
     PDEAVAIGAA IQGGILGKET TVKDLLLLDV TPLSLGLETL GGVFTKIIER NTTLPTSKTQ
     TFSTASDGQT VVEIAVYQGE RPIAKDNKQL ACFELTGIAP APRGVPQIDV TFDIDANGIL
     SVSAVDRATG RQQSVRITNR GGLSSMEIER MRQEAQIYAQ VDQIKKEIAE LRNQADALLY
     SYESTIKNHG ITLSPELRAR IEPVVQSMQA AMVDDNITPD EIRKRMEALQ QALVTLGSVV
     YQQTAGGSMM TSTPTMGRAT MSSQATQVLD SEATIISDNE ETVVSDYEAV D