ID   DNAK_PSYCK              Reviewed;         647 AA.
AC   Q1Q7X0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=Pcryo_2456;
OS   Psychrobacter cryohalolentis (strain ATCC BAA-1226 / DSM 17306 / VKM B-2378
OS   / K5).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Psychrobacter.
OX   NCBI_TaxID=335284;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1226 / DSM 17306 / VKM B-2378 / K5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Sims D.R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Richardson P.;
RT   "Complete sequence of chromosome of Psychrobacter cryohalolentis K5.";
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000323; ABE76233.1; -; Genomic_DNA.
DR   RefSeq; WP_011514754.1; NC_007969.1.
DR   AlphaFoldDB; Q1Q7X0; -.
DR   SMR; Q1Q7X0; -.
DR   STRING; 335284.Pcryo_2456; -.
DR   PRIDE; Q1Q7X0; -.
DR   KEGG; pcr:Pcryo_2456; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000002425; 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; SSF100934; SSF100934; 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..647
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059637"
FT   REGION          606..634
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        612..626
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   647 AA;  69505 MW;  44504D38B2E14409 CRC64;
     MGKVIGIDLG TTNSCVAVME GDKVKIIENA EGTRTTPSIV AYKDDEILVG QSAKRQAVTN
     PNNTLFAIKR LIGRRFDDKV VQKDIGMVPY KIAKADNGDA WVEINGKKLA PPQVSAEILK
     KMKKTAEDYL GEAVTEAVVT VPAYFNDSQR QATKDAGKIA GLDVKRIINE PTAAALAYGM
     DKKQGDSTVA VYDLGGGTFD VSIIEIADVD GEQQFEVLAT NGDTFLGGED FDSALIDFLV
     AEFKKDQDVN LKGDSLAMQR LKEAAEKAKI ELSSAQSTEV NLPYITADSS GPKHLVVTIS
     RSKLESLTEE LVQRTMGPCK IALEDAGIKI GDIDDVILVG GQTRMPLVQQ KVQEFFGQEP
     RKDVNPDEAV AAGAAIQGAV LSGEKTDVLL LDVTPLTLGI ETMGGILTPI IEKNTMIPTK
     KSQVFSTAED NQPAVSIQVY QGERKIANQN KQLGRFDLTD IPPAPRGLPQ IEVSFDINAD
     GIMNISATDK GTGKAQSIQI KADSGLSDEE VEQMIRDAEA NAAEDEKFAN LAQVRNEADG
     RIHAVQKALK DAADKVSDDE KSSVEAAISE LEAAAKEDDH EEIKAKLEAL DNAFLPVSQK
     IYADAGASAE GMDPNQFQQG ADNAGESNQA DDDVVDAEFT EVEDDKK