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Database: UniProt
Entry: DNAK_FRAAA
LinkDB: DNAK_FRAAA
Original site: DNAK_FRAAA 
ID   DNAK_FRAAA              Reviewed;         609 AA.
AC   Q0RBC4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 101.
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=FRAAL6639;
OS   Frankia alni (strain DSM 45986 / CECT 9034 / ACN14a).
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=326424;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45986 / CECT 9034 / ACN14a;
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA   Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA   Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA   Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA   Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA   Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA   Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(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; CT573213; CAJ65262.1; -; Genomic_DNA.
DR   RefSeq; WP_011607676.1; NC_008278.1.
DR   AlphaFoldDB; Q0RBC4; -.
DR   SMR; Q0RBC4; -.
DR   STRING; 326424.FRAAL6639; -.
DR   KEGG; fal:FRAAL6639; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_11; -.
DR   OrthoDB; 9766019at2; -.
DR   Proteomes; UP000000657; 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   CDD; cd10234; HSPA9-Ssq1-like_NBD; 1.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 3.30.420.40; -; 2.
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   NCBIfam; TIGR02350; prok_dnaK; 1.
DR   PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR   PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
DR   SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 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   Reference proteome; Stress response.
FT   CHAIN           1..609
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059560"
FT   REGION          572..609
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         175
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   609 AA;  65061 MW;  7B39E1D56BE6A4D3 CRC64;
     MARAVGIDLG TTNSVVSVLE GGEPTVIANA EGSRTTPSVV AFAKNGEVLV GEVAKRQAVT
     NVERTIRSVK RHMGTDWKMK VDAKDLTPQE ISAFILQKLK RDAESYLGET VADAVITVPA
     YFDDAQRQAT TEAGTIAGLN VLRIVNEPTA AALAYGLDKG EKEQTILVFD LGGGTFDVSL
     LEIGDGVVEV KSTSGDTHLG GDDWDQRITD HLIKTFNGQH GVDLGKDKMA LQRLREAAEK
     AKIELSQSSQ TSINLPYITA SAEGPLHLDV SLTRAEFQRM TSDLIDRCKH PFQQAVKDAG
     IKVSDIDHVV LVGGSTRMPA VVDLVRDLTG GKEPNKGVNP DEVVAVGASL QAGVLKGEVK
     DVLLLDVTPL SLGIETKGGI MTKLIERNTT IPTKRSEIFT TAEDSQPSVQ IQVFQGEREM
     AAYNKKLGMF ELTGLPPAPR GLPQIEVTFD IDANGIVHVS AKDLGTGKEQ SMTITGGSAL
     PRDDIDRMVR DAEQYAEEDR NRREEAETRN KAETLVYSTE RFLAENGEKI DAAVKSDVEE
     KLGTLRGAVA GTDTAAIREA ADALAAASQA MGQAMYEQAA QDGAGAPGSG GPADDDVVDA
     EIVDEEDKK
//
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