ID   DNAK_APHHA              Reviewed;         721 AA.
AC   O52960;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Chaperone protein DnaK;
DE   AltName: Full=HSP70;
DE   AltName: Full=Heat shock 70 kDa protein;
DE   AltName: Full=Heat shock protein 70;
GN   Name=dnaK; Synonyms=dnaK1;
OS   Aphanothece halophytica.
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Aphanothecaceae; Aphanothece.
OX   NCBI_TaxID=72020;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9426597; DOI=10.1023/a:1005867420619;
RA   Lee B.H., Hibino T., Jo J., Viale A.M., Takabe T.;
RT   "Isolation and characterization of a dnaK genomic locus in a halotolerant
RT   cyanobacterium Aphanothece halophytica.";
RL   Plant Mol. Biol. 35:763-775(1997).
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC   -!- INDUCTION: By stress conditions e.g. heat shock and by hyperosmotic
CC       environments.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; D84421; BAA24445.1; -; Genomic_DNA.
DR   AlphaFoldDB; O52960; -.
DR   SMR; O52960; -.
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   2: Evidence at transcript level;
KW   ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein;
KW   Stress response.
FT   CHAIN           1..721
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078411"
FT   REGION          606..649
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          667..721
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        632..649
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        691..721
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         197
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   721 AA;  79117 MW;  451D20C69963B2E8 CRC64;
     MGKVIGIDLG TTNSCFAVLE GGKPLVIENV EGGRTTPSIV AFTKEKERLV GQLAKRQAVT
     NAENTIYSIK RFIGRRWEDT EQERNRVSYH CVPGRDKTVD VKCWGKQYTP QELSAMILQT
     LKAGAEAYLN ETVTEAVITV PAYFTDAQRQ ATKDAGTIAG LNVMRIINEP TAAALAFGLD
     KQEQREQVLV YDLGGGTLDV SILQLGDGVF EVKATAGNNH LGGDDFDNVI VEWMLSEFQA
     QEGINLNEDK MAMQRLREAA ERAKIELSTR PTTSINLPFI TAFSKGGGEV GPKHLKLNLS
     RAKFNELSRP LVEKTIDPLK QAIEDSGLSV DQIDRILLVG GSTRIPEVQE ALKKFFNGKE
     PDRSINPDEA VALGAAIQGG VLGQEQEVED LLLLVVIPLS LGIETLGEVF TKVIERNTTI
     PTSKSQVFST ASDGQTSVEI HVLQGERAMA NDNKTLGKFL LTGIPAAPRG VPQIEVSFDI
     DVNGILKVSA EDKGTGREQG IVIKETGGLS QQEIERMQQE AEQYADEDRK RMQRIELSNQ
     ADSLFYSHEA TLKDNQGLIP QKVKATANKK KEELMAILED PNVELGVIQT RLEDYRQAVL
     SMGSEVYSQG SSKSSARDYE TVGEEEMTRE TGNSQESNAA FSTQPEGTVN NDNLELEAVF
     STYNDHTQGS DVATSSHDEI DLGDASDNSQ TNFDLDDEDF NPFEDFDEEE EASTDDYEAV
     E