DNAK_FRATW
ID DNAK_FRATW Reviewed; 642 AA.
AC A4IX28;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-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}; OrderedLocusNames=FTW_0571;
OS Francisella tularensis subsp. tularensis (strain WY96-3418).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=418136;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WY96-3418;
RX PubMed=17895988; DOI=10.1371/journal.pone.0000947;
RA Beckstrom-Sternberg S.M., Auerbach R.K., Godbole S., Pearson J.V.,
RA Beckstrom-Sternberg J.S., Deng Z., Munk C., Kubota K., Zhou Y., Bruce D.,
RA Noronha J., Scheuermann R.H., Wang A., Wei X., Wang J., Hao J.,
RA Wagner D.M., Brettin T.S., Brown N., Gilna P., Keim P.S.;
RT "Complete genomic characterization of a pathogenic A.II strain of
RT Francisella tularensis subspecies tularensis.";
RL PLoS ONE 2:E947-E947(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; CP000608; ABO46480.1; -; Genomic_DNA.
DR RefSeq; WP_003025465.1; NC_009257.1.
DR AlphaFoldDB; A4IX28; -.
DR SMR; A4IX28; -.
DR KEGG; ftw:FTW_0571; -.
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..642
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000059566"
FT REGION 614..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..642
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 201
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 642 AA; 69254 MW; 8236EAE6BC80336E CRC64;
MGKIIGIDLG TTNSCLAIMD GKTAKVIENA EGHRTTPSVV AYTDSGEILV GQAAKRQAVT
NPDNTFFAIK RLIGRKYDDK AVQEDIKKKV PYAVIKADNG DAWVATKEGK KMAPPQVSAE
VLRKMKKTAE DYLGEPVTEA VITVPAYFND SQRQATKDAG KIAGLEVKRI INEPTAAALA
YGVDSKKGEQ TVAVYDLGGG TFDISIIEIA DVDGDNQIEV LSTNGDTFLG GEDFDLALMN
YLIDEFKKEQ GIDLHNDKLA LQRVREAAEK AKVELSSAQQ TDVNLPYITA DATGPKHLNI
KVTRAKFESL VSDLVMRSLE PCKKALEDAG LSKSDITEVL LVGGQTRMPL VQEKVKEFFG
KEPRKDVNPD EAVAVGAAIQ GGVLSGDVKD ILLLDVTPLS LGIETMGGVM TKLIERNTTI
PTKKSQVFST AEDNQPAVTI HVLQGEREMA SANKSLGRFD LADIPPAPRG MPQIEVTFDI
DANGILNVSA KDKATGKEQN IVIKSSSGLS EEDIEKMVQD AEANAEADKK FHDLVTARNT
ADNLIHSSRK AIQELGDKVT AAEKEKIEEA CKELEAATKG DDKQAIEAKT KALEEAFAPI
AQKAYAEQAQ AAVAQGGAKA EEPKKEEDVV DADFEDVEDD KK