DNAK_FRAP2
ID DNAK_FRAP2 Reviewed; 642 AA.
AC B0TYF2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=Fphi_1403;
OS Francisella philomiragia subsp. philomiragia (strain ATCC 25017 / FSC 153 /
OS O#319-036).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=484022;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25017 / FSC 153 / O#319-036;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Richardson P.;
RT "Complete sequence of chromosome of Francisella philomiragia subsp.
RT philomiragia ATCC 25017.";
RL Submitted (DEC-2007) 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; CP000937; ABZ87628.1; -; Genomic_DNA.
DR RefSeq; WP_012280751.1; NC_010336.1.
DR AlphaFoldDB; B0TYF2; -.
DR SMR; B0TYF2; -.
DR STRING; 484022.Fphi_1403; -.
DR EnsemblBacteria; ABZ87628; ABZ87628; Fphi_1403.
DR KEGG; fph:Fphi_1403; -.
DR eggNOG; COG0443; Bacteria.
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_1000079227"
FT REGION 607..642
FT /note="Disordered"
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; 69168 MW; 6F261D340D51C0EF CRC64;
MGKIIGIDLG TTNSCLAIMD GKTAKVIENA EGHRTTPSVV AYTDNGEILV GQAAKRQAVT
NPDNTFFAIK RLIGRKYDDK AVQEDIKKKV PYAVIKADNG DAWVATKEGK KMAPPQVSAE
VLRKMKKTAE DYLGEPVTEA VITVPAYFND SQRQATKDAG KIAGLEVKRI INEPTAAALA
YGVDSKKGEQ TVAVYDLGGG TFDISIIEIA DVDGDNQIEV LSTNGDTFLG GEDFDVALMN
YLIDEFKKEQ GIDLHNDKLA LQRVREAAEK AKVELSSAQQ TDVNLPYITA DATGPKHLNI
KVTRAKFESL VSDLVMRSLE PCKKALEDAG LSKSDITEVL LVGGQTRMPL VQEKVKEFFG
KEPRKDVNPD EAVAVGAAIQ GGVLAGDVKD VLLLDVTPLS LGIETMGGVM TKLIERNTTI
PTKKSQVFST AEDNQPAVTI HVLQGEREMA SANKSLGRFD LADIPPAPRG IPQIEVTFDI
DANGILNVSA KDKATGKEQN IVIKSSSGLS EDDIEKMVQD AEANAESDKK FHELVSARNT
ADNLIHSSRK AIAELGDKVS AEEKEKVEEA CKDLESVVKG DDKDAIDAKT KALEEVFSPI
AQKAYAEQAQ AAGAQGGAQA EEPKKDDDVV DADFEDVEDN KK