ID   DNAK_SHEDO              Reviewed;         638 AA.
AC   Q12Q08;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=Sden_1182;
OS   Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS217 / ATCC BAA-1090 / DSM 15013;
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   Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of Shewanella denitrificans OS217.";
RL   Submitted (MAR-2006) 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; CP000302; ABE54468.1; -; Genomic_DNA.
DR   RefSeq; WP_011495628.1; NC_007954.1.
DR   AlphaFoldDB; Q12Q08; -.
DR   SMR; Q12Q08; -.
DR   STRING; 318161.Sden_1182; -.
DR   PRIDE; Q12Q08; -.
DR   EnsemblBacteria; ABE54468; ABE54468; Sden_1182.
DR   KEGG; sdn:Sden_1182; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000001982; 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..638
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059661"
FT   REGION          602..638
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   638 AA;  68790 MW;  D2D5B71014B8188F CRC64;
     MGKIIGIDLG TTNSCVAVLD GGKARVLENA EGDRTTPSIV AYTDEEIIVG QPAKRQAVTN
     PNNTFFAIKR LIGRRFKDDE VQRDVDIMPF KIIGADNGDA WVEQRGNKMA PPQVSAEILK
     KMKKTAEDFL GEEVTEAVIT VPAYFNDSQR QATKDAGRIA GLEVKRIINE PTAAALAYGI
     DKKQGDNIVA VYDLGGGTFD ISIIEIDSND GDQTFEVLAT NGDTHLGGED FDNRLINYLA
     DEFKKDQGLD LRRDPLAMQR LKEAAEKAKI ELSSTNQTEV NLPYITADAS GPKHLVVKVT
     RTKLESLVED LIQRTLEPLK VALADADLSV SEINEVILVG GQTRMPKVQE AVTNFFGKEP
     RKDVNPDEAV AVGAAIQAGV LSGEVKDVLL LDVTPLSLGI ETMGSVMTKL IDKNTTIPTK
     AQQVFSTADD NQSAVTIHVL QGERKQASAN KSLGQFNLEG IEPAPRGQPQ VEVMFDIDAD
     GILHVSATDK KTGKKQNITI KASSGLSDEE VEQMVRDAEA HADEDAKFEA LVQARNQADG
     LVHATKKQVT EAGDALASDE KEKIEAAMAA VDEATKGKDA EAIEKATQAL IEASAKLMEI
     AQAKSQAQGG EEAQAKDAGQ SNDDVVDAEF EEVKDDKK