ID   DNAK_BACP2              Reviewed;         613 AA.
AC   A8FFD2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=BPUM_2280;
OS   Bacillus pumilus (strain SAFR-032).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=315750;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAFR-032;
RX   PubMed=17895969; DOI=10.1371/journal.pone.0000928;
RA   Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D.,
RA   Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H.,
RA   Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y.,
RA   Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P.,
RA   Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D.,
RA   Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F.,
RA   Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K.,
RA   Weinstock G.M.;
RT   "Paradoxical DNA repair and peroxide resistance gene conservation in
RT   Bacillus pumilus SAFR-032.";
RL   PLoS ONE 2:E928-E928(2007).
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; CP000813; ABV62949.1; -; Genomic_DNA.
DR   RefSeq; WP_012010629.1; NZ_VEIS01000005.1.
DR   AlphaFoldDB; A8FFD2; -.
DR   SMR; A8FFD2; -.
DR   STRING; 315750.BPUM_2280; -.
DR   PRIDE; A8FFD2; -.
DR   EnsemblBacteria; ABV62949; ABV62949; BPUM_2280.
DR   KEGG; bpu:BPUM_2280; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_9; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000001355; 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; 2.
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..613
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059510"
FT   REGION          577..613
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        595..613
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         173
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   613 AA;  66114 MW;  1587BCC9162E1EAF CRC64;
     MSKIIGIDLG TTNSCVAVLE GGEPKVIANA EGARTTPSVV AFKNGERQVG EVAKRQSITN
     PNTIMSVKRH MGTDYKVEVE GKNYTPQEIS AIILQHLKSY AEGYLGEEVT KAVITVPAYF
     NDAERQATKD AGKIAGLEVE RIINEPTAAA LAYGLDKTDE DQTILVYDLG GGTFDVSVLE
     LGDGVFEVRS TAGDNRLGGD DFDQVIIDHL VAEFKKENGI DLSKDKMALQ RLKDAAEKAK
     KDLSGVSSTQ ISLPFITAGD AGPLHLELTL TRAKFEELSA DLVERTMTPV RQSLKDAGLS
     ASEIDKVILV GGSTRIPAVQ EAIKKETGKE PHKGVNPDEV VALGAAIQGG VITGDVKDVV
     LLDVTPLSLG IETMGGVFTK LIERNTTIPT SKSQVFSTAA DNQTAVDIHV LQGERPMAAD
     NKTLGRFQLT DIPPAPRGVP QIEVSFDIDK NGIVNVRAKD MGTGKEQNIT IKSSSGLSDD
     EIEKMVKEAE ENAEADAKKK EEIEVRNEAD QLVFTTEKTL KDLEGKIDEE QVKKANDAKD
     ALKAAIEKGE LEDIKAKKDE LQTIVQELTT KLYEEAAKQA QAQQEGGAEG AQKADDNVVD
     AEYEEVNDDQ EKK