ID   DNAK_CUTAC              Reviewed;         617 AA.
AC   P0CY98; Q9L7P1;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Chaperone protein DnaK;
DE   AltName: Full=HSP70;
DE   AltName: Full=Heat shock 70 kDa protein;
DE   AltName: Full=Heat shock protein 70;
GN   Name=dnaK;
OS   Cutibacterium acnes (Propionibacterium acnes).
OC   Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC   Cutibacterium.
OX   NCBI_TaxID=1747;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=P37;
RA   Farrar M.D., Ingham E., Holland K.T.;
RT   "Cloning and sequencing of a dnaK homolog from Propionibacterium acnes.";
RL   Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC   -!- INDUCTION: By stress conditions e.g. heat shock (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; AF222062; AAF33789.1; -; Genomic_DNA.
DR   RefSeq; WP_002514483.1; NZ_WOWJ01000004.1.
DR   AlphaFoldDB; P0CY98; -.
DR   SMR; P0CY98; -.
DR   PRIDE; P0CY98; -.
DR   GeneID; 66621944; -.
DR   PATRIC; fig|1747.45.peg.539; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
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; 2.
DR   Pfam; PF00012; HSP70; 2.
DR   SUPFAM; SSF100920; SSF100920; 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..617
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000410485"
FT   REGION          578..617
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        579..601
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         175
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   617 AA;  66363 MW;  F217F4C9D3453F27 CRC64;
     MARSVGIDLG TTNSCVAVLE GGEPTVIPNA EGARTTPSVV AFTNSGETLV GEVAKRQAVT
     NVDRTVRSVK RHMGEAWTMG VDDKTYKPQQ ISAFILQKLK RDAEAYLGEP VTNAVITVPA
     YFSDAQRQAT KEAGEIAGLA VDRIVNEPTA AALAYGLDKT DKDQTVLVFD LGGGTFDVSL
     LDISDGVFEV KATNGDNHLG GDDWDQRIVD WLVTQFKNAN GIDLAADKMA KQRLQEAAER
     AKIELSQASE THINLPYITA GAAGPLHLDE KLTRAEFQRM TSDLLERCRT PFNAVMKDAG
     LNVSQIDEVI LVGGSTRMPA VAELVKELAG KDPHKGVNPD EVVALGASLQ AGVLKGEVKD
     VLLLDVTPLS LGIETKGGVM TKIIERNTTI PTKRSEVFTT AEDNQPSVMI QVFQGEREFV
     RDNKSLGNFE LTGLMPAPRG IPQIEVSFDI DANGIVHVHA KDMATGKEQS MTVTGGSALG
     KDEIDRMVKE AEANAEADKK RREAVEMRNE ADALAFRTEK LLDENSDKIP EDTKTPVTEA
     IATLKETLKG TDNDDEVKAA MDDLNQKASA MGQAIYAAAQ QAQAENPQGQ DAESASSESG
     DDTVVDAEIV DDEDEKK