ID   DNAK_SHEB8              Reviewed;         639 AA.
AC   A6WRU9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
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};
GN   OrderedLocusNames=Shew185_3411;
OS   Shewanella baltica (strain OS185).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=402882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS185;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Brettar I., Rodrigues J., Konstantinidis K., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome of Shewanella baltica OS185.";
RL   Submitted (JUL-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; CP000753; ABS09538.1; -; Genomic_DNA.
DR   RefSeq; WP_011847566.1; NC_009665.1.
DR   AlphaFoldDB; A6WRU9; -.
DR   SMR; A6WRU9; -.
DR   KEGG; sbm:Shew185_3411; -.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; ISIKRHM; -.
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   Stress response.
FT   CHAIN           1..639
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059660"
FT   REGION          602..639
FT                   /note="Disordered"
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   639 AA;  68974 MW;  2A847A14B32F09EF CRC64;
     MGKIIGIDLG TTNSCVAVLD GGKARVLENA EGDRTTPSII AYTDDETIVG SPAKRQAVTN
     PTNTFFAIKR LIGRRFKDDE VQRDVNIMPF KIIAADNGDA WVESRGNKMA PPQVSAEILK
     KMKKTAEDFL GEEVTEAVIT VPAYFNDSQR QATKDAGRIA GLDVKRIINE PTAAALAYGI
     DKKQGDNIVA VYDLGGGTFD ISIIEIDSND GDQTFEVLAT NGDTHLGGED FDNRLINYLA
     DEFKKEQGLD LRKDPLAMQR LKEAAEKAKI ELSSTNHTEV NLPYITADAT GPKHLVIKIT
     RAKLESLVED LILRTLEPLK VALADADLSV TDINEVILVG GQTRMPKVQE AVTNFFGKEP
     RKDVNPDEAV AVGAAIQAGV LSGDVKDVLL LDVTPLSLGI ETMGSVMTKL IEKNTTIPTK
     AQQVFSTADD NQSAVTIHVL QGERKQASAN KSLGQFNLDG IEPAQRGQPQ IEVMFDIDAD
     GILHVSATDK KTGKKQNITI KASSGLSEEE VAQMVRDAEA HADEDKKFEE LVQSRNQADG
     LVHATKKQVE EAGDALPSED KEKIQAAMDA VDTAIKGNDK EAIEKATQEL IEASAKLMEI
     AQAKSQAQGG DNADAGKQAN ATADDVVDAE FEEVKDDKK