ID   DNAK_PROMH              Reviewed;         641 AA.
AC   B4F2V5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=PMI0009;
OS   Proteus mirabilis (strain HI4320).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=529507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HI4320;
RX   PubMed=18375554; DOI=10.1128/jb.01981-07;
RA   Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA   Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA   Parkhill J., Mobley H.L.T.;
RT   "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT   both adherence and motility.";
RL   J. Bacteriol. 190:4027-4037(2008).
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; AM942759; CAR40249.1; -; Genomic_DNA.
DR   RefSeq; WP_012367437.1; NC_010554.1.
DR   AlphaFoldDB; B4F2V5; -.
DR   SMR; B4F2V5; -.
DR   STRING; 529507.PMI0009; -.
DR   PRIDE; B4F2V5; -.
DR   EnsemblBacteria; CAR40249; CAR40249; PMI0009.
DR   GeneID; 6803160; -.
DR   KEGG; pmr:PMI0009; -.
DR   PATRIC; fig|529507.6.peg.9; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000008319; 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   Reference proteome; Stress response.
FT   CHAIN           1..641
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000119741"
FT   REGION          604..641
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        618..641
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         199
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   641 AA;  69283 MW;  34F871DACC4D6330 CRC64;
     MGKIIGIDLG TTNSCVAVMD GKNARVIENG EGDRTTPSIV AYAQDGEILV GQPAKRQAVT
     NSQNTLFAIK RLIGRRFEDA EVQRDVSIMP YKIIKADNGD AWVEARNEKM APPQVSAEVL
     KKMKKTAEDY LGEPVTEAVI TVPAYFNDAQ RQATKDAGRI AGLDVKRIIN EPTAAALAYG
     LDREVGNRTI AVYDLGGGTF DISIIEIDEV DGEKTYEVLS TNGDTHLGGE DFDSRLINYL
     VDEFKKEQGI DLRNDPLAMQ RLKEAAEKAK IELSSAQQTD VNLPYVTADA TGPKHLNIKV
     TRAKLESLVE DLVKRSMDPV KVALEDAGLK VSEVNDVILV GGQTRMPMVQ KTVAEFFGKE
     PRKDVNPDEA VAMGAAVQGG VLAGDVKDVL LLDVTPLSLG IETMGGVMTS LIAKNTTIPT
     KHSQVFSTAE DNQSAVTIHV LQGERKRASD NKSLGQFNLD GIQPAPRGMP QIEVTFDIDA
     DGILHVSAKD KNSGREQNIT IKASSGLNEE EIQKMVRDAE ANAEADRKFE ELVQTRNQAD
     QLVHGTRKQI EEAGDKLAAN DKEAIEKALS ELEIASKGED KAAIEAKLQA LVEASKPLLE
     IAQQQAQAGA GNTADATDAG AKKDDDVVDA EFEEVDGKDK K