DNAK_HAEI8
ID DNAK_HAEI8 Reviewed; 635 AA.
AC Q4QJW4;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=NTHI1929;
OS Haemophilus influenzae (strain 86-028NP).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=281310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=86-028NP;
RX PubMed=15968074; DOI=10.1128/jb.187.13.4627-4636.2005;
RA Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B.,
RA Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O.,
RA Munson R.S. Jr.;
RT "Genomic sequence of an otitis media isolate of nontypeable Haemophilus
RT influenzae: comparative study with H. influenzae serotype d, strain KW20.";
RL J. Bacteriol. 187:4627-4636(2005).
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; CP000057; AAX88683.1; -; Genomic_DNA.
DR RefSeq; WP_005694297.1; NC_007146.2.
DR AlphaFoldDB; Q4QJW4; -.
DR SMR; Q4QJW4; -.
DR EnsemblBacteria; AAX88683; AAX88683; NTHI1929.
DR KEGG; hit:NTHI1929; -.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000002525; 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..635
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000225969"
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; 68281 MW; 58167BFA0BA661C9 CRC64;
MGKIIGIDLG TTNSCVAVMD GDKARVIENA EGARTTPSII AYTDNETLVG QPAKRQAITN
PKNTLFAIKR LIGRRFESEE VQRDIKIMPF EITRADNGDA WVNVKGDKLA PPQISAEVLK
KMKKTAEDFL GESVTEAVIT VPAYFNDAQR QATIDAGKIA GLDVKRIINE PTAAALAFGL
GSSKENQVIA VYDLGGGTFD ISIIEIDNFD GEQTFEVLAT GGNTHLGGED FDNRVIDYII
DEFKKEQNID LRNDAMALQR VKEAAEKAKI ELSSAQSTEV NLPYITADAT GPKHLALNIT
RAKLEALVED LVASSIESLK AVLKDADKGV SEIHDIILVG GQTRMPLVQQ KVAEFFGKEA
RKDVNPDEAV AIGAAVQGGV LKGDVKDVLL LDVTPLSLGI ETMGGVMTTL IEKNTTIPTK
KSQVFSTAED NQSAVTIHVL QGERKRAADN KSLGQFNLEG INPAPRGMPQ IEVTFDIDAN
GVINVSAKDK NTGKEQQIRI QASSGLSDEE IQQMVRDAEA NADADRKFEE VVQARNQADG
IAHATRKQIA EAGDALSVAD KEKIEAAVAE LETAAKGEDK AEIEAKIEAV IKASEPLMQA
VQAKAQQAGG EQPQQSSAKD DGVVDAEFEE VKDNK