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DNAK_FRATH
ID   DNAK_FRATH              Reviewed;         642 AA.
AC   Q2A328;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=FTL_1191;
OS   Francisella tularensis subsp. holarctica (strain LVS).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=376619;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LVS;
RA   Chain P., Larimer F., Land M., Stilwagen S., Larsson P., Bearden S.,
RA   Chu M., Oyston P., Forsman M., Andersson S., Lindler L., Titball R.,
RA   Garcia E.;
RT   "Complete genome sequence of Francisella tularensis LVS (Live Vaccine
RT   Strain).";
RL   Submitted (MAR-2006) 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; AM233362; CAJ79630.1; -; Genomic_DNA.
DR   RefSeq; WP_003016262.1; NZ_CP009694.1.
DR   AlphaFoldDB; Q2A328; -.
DR   SMR; Q2A328; -.
DR   KEGG; ftl:FTL_1191; -.
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_1000059563"
FT   REGION          609..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;  69182 MW;  41308B011F9E9862 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 VLLLDVTPLS LGIETMGGVM TKLIERNTTI
     PTKKSQVFST AEDNQPAVTI HVLQGEREMA SANKSLGRFD LADIPPAPRG MPQIEVTFDI
     DANGILNVSA KDKATGKEQN IVIKSSSGLS EEDIEKMVQD AEANAEADKK FHDLVTARNT
     ADNLIHSSRK AIQELGDKVT AAEKEKIEEA CKELEAATKG DDKQAIEAKT KALEEAFAPI
     AQKAYAEQAQ AAGAQGGAKA EEPKKEEDVV DADFEDVEDD KK
 
 
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