ID   DNAK_PSYIN              Reviewed;         640 AA.
AC   A1STE4;
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=Ping_0917;
OS   Psychromonas ingrahamii (strain 37).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Psychromonadaceae; Psychromonas.
OX   NCBI_TaxID=357804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=37;
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   Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Staley J.,
RA   Richardson P.;
RT   "Complete sequence of Psychromonas ingrahamii 37.";
RL   Submitted (JAN-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; CP000510; ABM02759.1; -; Genomic_DNA.
DR   RefSeq; WP_011769322.1; NC_008709.1.
DR   AlphaFoldDB; A1STE4; -.
DR   SMR; A1STE4; -.
DR   STRING; 357804.Ping_0917; -.
DR   PRIDE; A1STE4; -.
DR   EnsemblBacteria; ABM02759; ABM02759; Ping_0917.
DR   KEGG; pin:Ping_0917; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000000639; 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..640
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059638"
FT   REGION          602..640
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   640 AA;  69615 MW;  0E89709638C056B9 CRC64;
     MGKIIGIDLG TTNSCVSVLV GGVAKIIENA EGERTTPSII AYTEGETLVG QPAKRQSVTN
     PQNTLFAIKR LIGRRYEDEE VQRDIKIMPY KIVKADNGDA WVEAHGNKMA PPQISAEVLK
     KMKKTAEDYL GEKVTGAVIT VPAYFNDAQR QATKDAGRIA GLEVKRIINE PTAAAFAYGV
     DSSKGDSVIA VYDLGGGTFD ISIIEIDEVD GEKTFEVLST NGDTHLGGED FDNRLINFLV
     AEFKTQQGFD LTNDPLAMQR VKEAAEKAKI ELSSAQQTDI NLPYITADQS GPKHLNIKIT
     RAKLESLVED MVKSTLEPLR IALKDADLSV ADIDDVILVG GQTRMPLVQK LVTEFFGKEA
     RKDVNPDEAV AMGAAIQGAV LSGEKTDVLL LDVTPLSLGI ETMGGVLTKV IDKNTTIPTK
     QSQTFSTAED NQSAVTIHIL QGERKRATDN KSLGQFNLEG IRKASRGTPQ IEVTFDMDAD
     GILHVSAQDK DTKQEQKITI KSSSGLSEEE VEKMVNDAEA NAEADKKFEE VVKARNQADA
     IVHTTRKQIE EAGDALPADE KEKIEAALKE LDEATKGEDK DIIEAKTTAV AEASEKLMEI
     VQQKAQAAEA GGEEQPKEKT KEEDDIVDAE FEEVKKDDKK