ID   DNAK_HAEIE              Reviewed;         635 AA.
AC   A5UBQ1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
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};
GN   OrderedLocusNames=CGSHiEE_03925;
OS   Haemophilus influenzae (strain PittEE).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=374930;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PittEE;
RX   PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103;
RA   Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C.,
RA   Ehrlich G.D.;
RT   "Characterization and modeling of the Haemophilus influenzae core and
RT   supragenomes based on the complete genomic sequences of Rd and 12 clinical
RT   nontypeable strains.";
RL   Genome Biol. 8:R103.1-R103.18(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; CP000671; ABQ98202.1; -; Genomic_DNA.
DR   RefSeq; WP_011961899.1; NC_009566.1.
DR   AlphaFoldDB; A5UBQ1; -.
DR   SMR; A5UBQ1; -.
DR   KEGG; hip:CGSHiEE_03925; -.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; ISIKRHM; -.
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_1000059571"
FT   REGION          602..635
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        605..619
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   635 AA;  68237 MW;  3419B405D40DA52B CRC64;
     MGKIIGIDLG TTNSCVAVMD GDKARVIENA EGARTTPSII AYTDNETLVG QPAKRQAITN
     PKNTLFAIKR LIGRRFESEE VQRDIKIMPF EITRADNGDA WVNVKGDKLA PPQISAEVLK
     KMKKTAEDFL GEAVTEAVIT VPAYFNDAQR QATIDAGKIA GLDVKRIINE PTAAALAFGL
     GSSKENQVIA VYDLGGGTFD ISIIEIDNFD GEQTFEVLAT GGNTHLGGED FDNRVIDYII
     DEFKKEQNID LRNDAMALQR VKEAAEKAKI ELSSAQSTEV NLPYITADAT GPKHLALNIT
     RAKLEALVED LVASSIESLK AVLKDAGKGV SEIHDIILVG GQTRMPLVQQ KVAEFFGKEA
     RKDVNPDEAV AIGAAVQGGV LKGDVKDVLL LDVTPLSLGI ETMGGVMTTL IEKNTTIPTK
     KSQVFSTAED NQSAVTIHVL QGERKRAADN KSLGQFNLEG INPAPRGMPQ IEVTFDIDAN
     GVINVSAKDK NTGKEQQIRI QASSGLSDEE IQQMVRDAEA NADADRKFEE VVQARNQADG
     IAHATRKQIA EAGDALSVAD KEKIETAVAE LETAAKGEDK AEIEAKIEAV IKASEPLMQV
     AQAKAQQAGG EQPQQSSAKD DGVVDAEFEE VKDNK