ID   DNAK_HISS2              Reviewed;         635 AA.
AC   B0UWR4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-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=HSM_0368;
OS   Histophilus somni (strain 2336) (Haemophilus somnus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=228400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2336;
RG   US DOE Joint Genome Institute;
RA   Siddaramappa S., Duncan A.J., Challacombe J.F., Rainey D., Gillaspy A.F.,
RA   Carson M., Gipson J., Gipson M., Bruce D., Detter J.C., Han C.S., Land M.,
RA   Tapia R., Thompson L.S., Orvis J., Zaitshik J., Barnes G., Brettin T.S.,
RA   Dyer D.W., Inzana T.J.;
RT   "Complete sequence of Haemophilus somnus 2336.";
RL   Submitted (FEB-2008) 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; CP000947; ACA32005.1; -; Genomic_DNA.
DR   RefSeq; WP_012341224.1; NC_010519.1.
DR   AlphaFoldDB; B0UWR4; -.
DR   SMR; B0UWR4; -.
DR   STRING; 228400.HSM_0368; -.
DR   EnsemblBacteria; ACA32005; ACA32005; HSM_0368.
DR   KEGG; hsm:HSM_0368; -.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
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..635
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000079230"
FT   REGION          600..635
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        600..621
FT                   /note="Polar 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   635 AA;  68489 MW;  4BC6BAB859FC7520 CRC64;
     MGKIIGIDLG TTNSCVAVMD GDKPRVIENA EGERTTPSII AYTNDNETLV GQPAKRQAVT
     NPKNTLFAIK RLIGRRFEDQ EVQRDVAIMP FEITKADNGD AWVSVKGEKM APPQISAEVL
     KKMKKTAEDF LGETVTEAVI TVPAYFNDAQ RQATKDAGRI AGLEVKRIIN EPTAAALAYG
     LDKGKGNQTI AVYDLGGGTF DLSIIEIDEV GGEKTFEVLA TNGDTHLGGE DFDNRVINYL
     VDEFKKEQGV DLRNDPLAMQ RLKEAGEKAK IELSSAQQTD VNLPYITADA TGPKHLNIKL
     TRAKLEALVE DLVARSMEPV KVALSDAGLS VSEINDVILV GGQTRMPLVQ QKVAEFFGKE
     PRRDVNPDEA VAIGAAVQGG VLAGDVKDVL LLDVTPLSLG IETMGGVMTT LIEKNTTIPT
     KKSQVFSTAE DNQSAVTIHV LQGERKQASA NKSLGQFNLE GINPAPRGMP QIEVTFDIDA
     DGIIHVSAKD KGTGKEQKIT IKASSGLSDE EIQQMVRDAE ANAEADRKFE ELVQARNQAD
     HLVHSTRKQL AEVGEKLSAE DKAPIESAVN ELETAAKGED KTEIDAKVQA LIQVSEKLLQ
     ASQQQAQADA GAQQSQSTKG GEDVVDAEFE EVKDK