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DNAK_FRAT1
ID   DNAK_FRAT1              Reviewed;         642 AA.
AC   Q14GW9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, 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=FTF1269c;
OS   Francisella tularensis subsp. tularensis (strain FSC 198).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=393115;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSC 198;
RX   PubMed=17406676; DOI=10.1371/journal.pone.0000352;
RA   Chaudhuri R.R., Ren C.-P., Desmond L., Vincent G.A., Silman N.J.,
RA   Brehm J.K., Elmore M.J., Hudson M.J., Forsman M., Isherwood K.E.,
RA   Gurycova D., Minton N.P., Titball R.W., Pallen M.J., Vipond R.;
RT   "Genome sequencing shows that European isolates of Francisella tularensis
RT   subspecies tularensis are almost identical to US laboratory strain Schu
RT   S4.";
RL   PLoS ONE 2:E352-E352(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; AM286280; CAL09285.1; -; Genomic_DNA.
DR   RefSeq; WP_003021930.1; NC_008245.1.
DR   AlphaFoldDB; Q14GW9; -.
DR   SMR; Q14GW9; -.
DR   KEGG; ftf:FTF1269c; -.
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_1000059561"
FT   REGION          615..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;  82229906BC8E968E 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 GGVLAGDVKD ILLLDVTPLS LGIETMGGVM TKLIERNTTI
     PTKKSQVFST AEDNQPAVTI HVLQGEREMA SANKSLGRFD LADIPPAPRG MPQIEVTFDI
     DANGILNVSA KDKATGKEQN IVIKSSSGLS EEDIEKMVQD AEANAEADKK FHDLVTARNT
     ADNLIHSSRK AIQELGDKVT AAEKEKIEEA CKELEAATKG DDKQAIESKT KALEEAFAPI
     AQKAYAEQAQ AAVAQGGAKA EEPKKEEDVV DADFEDVEDD KK
 
 
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