ID   DNAK_SHEAM              Reviewed;         637 AA.
AC   A1S8K7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=Sama_2511;
OS   Shewanella amazonensis (strain ATCC BAA-1098 / SB2B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=326297;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1098 / SB2B;
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   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Fredrickson J.,
RA   Richardson P.;
RT   "Complete sequence of Shewanella amazonensis SB2B.";
RL   Submitted (DEC-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; CP000507; ABM00714.1; -; Genomic_DNA.
DR   RefSeq; WP_011760620.1; NC_008700.1.
DR   AlphaFoldDB; A1S8K7; -.
DR   SMR; A1S8K7; -.
DR   STRING; 326297.Sama_2511; -.
DR   PRIDE; A1S8K7; -.
DR   EnsemblBacteria; ABM00714; ABM00714; Sama_2511.
DR   KEGG; saz:Sama_2511; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000009175; 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..637
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059658"
FT   REGION          604..637
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        604..618
FT                   /note="Polar residues"
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   637 AA;  68486 MW;  0310ECE4D55939BD CRC64;
     MGKIIGIDLG TTNSCVAVLD GGKARVIENA EGDRTTPSII AFTEDETLVG QPAKRQAVTN
     PTNTFFAIKR LIGRRFKDDE VQRDVNIMPF KIIQADNGDA WVESRGKKMA PPQVSAEVLK
     KMKKTAEDFL GEEVTEAVIT VPAYFNDAQR QATKDAGRIA GLDVKRIINE PTAAALAYGI
     DKKQGDNIVA VYDLGGGTFD ISIIEIDNND GDQTFEVLAT NGDTHLGGED FDNRLINYLA
     DEFKKEQGLD LRNDPLAMQR LKEAAEKAKI ELSSTNQTEV NLPYITADAT GPKHLVVKVT
     RAKLESLVED LIQRSLEPLK VALADADLSV SDINEVILVG GQTRMPKVQE AVTNFFGKEP
     RKDVNPDEAV AVGAAVQAGV LAGDVKDVLL LDVTPLSLGI ETMGSVMTKL IEKNTTIPTK
     ASQVFSTADD NQSAVTIHVL QGERKQASAN KSLGQFNLEG IEPAPRGMPQ IEVTFDIDAD
     GILHVSAKDK KTGKEQKITI KASSGLSDEE VAQMVRDAEA HADEDKKFEE LAQARNQADG
     LVHATKKQVE EAGDALGSDD KAKIEAAIAE VEKAVKGNDK EAIDTATQSL IEASAKLVEI
     AQAKAQGAQS SAQGSSAEKT ADDVVDAEFE EVKDDKK