ID   DNAK_SHESW              Reviewed;         639 AA.
AC   A1RGN1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=Sputw3181_0976;
OS   Shewanella sp. (strain W3-18-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=351745;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W3-18-1;
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   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella sp. W3-18-1.";
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; CP000503; ABM23826.1; -; Genomic_DNA.
DR   RefSeq; WP_011788352.1; NC_008750.1.
DR   AlphaFoldDB; A1RGN1; -.
DR   SMR; A1RGN1; -.
DR   GeneID; 45043468; -.
DR   KEGG; shw:Sputw3181_0976; -.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000002597; 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   Stress response.
FT   CHAIN           1..639
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059668"
FT   REGION          605..624
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;  68855 MW;  F0ED47F5D495A742 CRC64;
     MGKIIGIDLG TTNSCVAVLD GGKARVLENA EGDRTTPSII AYTDDETIVG SPAKRQAVTN
     PTNTFFAIKR LIGRRFKDDE VQRDVNIMPF KIIQADNGDA WVESRGNKMA PPQVSAEILK
     KMKKTAEDFL GEEVTEAVIT VPAYFNDSQR QATKDAGRIA GLDVKRIINE PTAAALAYGI
     DKKQGDNIVA VYDLGGGTFD ISIIEIDSND GDQTFEVLAT NGDTHLGGED FDNRLINYLA
     DEFKKEQGLD LRKDPLAMQR LKEAAEKAKI ELSSTNHTEV NLPYITADAT GPKHLVIKIT
     RAKLESLVED LILRTLEPLK VALADADLSV SDVNEVILVG GQTRMPKVQE AVTNFFGKEP
     RKDVNPDEAV AVGAAIQAGV LSGDVKDVLL LDVTPLSLGI ETMGSVMTKL IEKNTTIPTK
     AQQVFSTADD NQSAVTIHVL QGERKQASAN KSLGQFNLDG IEPAPRGQPQ IEVMFDIDAD
     GILHVSATDK KTGKKQNITI KASSGLSEEE VAQMVRDAEA HADEDKKFEE LVQARNQADG
     LVHATKKQVE EAGDALPSED KEKIQAAMAA VDTATKGNDK EAIEKASQEL IEASAKLMEI
     AQAKSQAQGG AETNAGKQAN AAADDVVDAE FEEVKDDKK