ID   DNAK_ERYRH              Reviewed;         600 AA.
AC   Q05647;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   03-AUG-2022, entry version 97.
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   Erysipelothrix rhusiopathiae.
OC   Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales;
OC   Erysipelotrichaceae; Erysipelothrix.
OX   NCBI_TaxID=1648;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=E1-6P;
RX   PubMed=8423071; DOI=10.1128/iai.61.2.411-417.1993;
RA   Partridge J., King J., Blum P.;
RT   "Cloning, heterologous expression, and characterization of the
RT   Erysipelothrix rhusiopathiae DnaK protein.";
RL   Infect. Immun. 61:411-417(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 592-600.
RC   STRAIN=E1-6P;
RX   PubMed=8359682; DOI=10.1111/j.1574-6968.1993.tb06365.x;
RA   Rockabrand D., Partridge J., Krska J., Blum P.;
RT   "Nucleotide sequence analysis and heterologous expression of the
RT   Erysipelothrix rhusiopathiae dnaJ gene.";
RL   FEMS Microbiol. Lett. 111:79-85(1993).
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; M98865; AAA24869.1; -; Genomic_DNA.
DR   EMBL; L08110; AAA71921.1; -; Unassigned_DNA.
DR   PIR; A49230; A49230.
DR   AlphaFoldDB; Q05647; -.
DR   SMR; Q05647; -.
DR   PRIDE; Q05647; -.
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; 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..600
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078463"
FT   REGION          569..600
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        569..586
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         173
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   600 AA;  64583 MW;  63168067C17ACF79 CRC64;
     MSKVIGIDLG TTNSAVSVMD GGEAKVITNP EGNRTTPSVV SFKNGERIVG DAAKRQVVTN
     PNSAVSVKRL IGTGEKVTLE GKDYTPEEIS AMILGYMKSY AEDYLGEKVT KAVITVPAYF
     NDAQRQATKD AGKIAGLEVE RIINEPTAAA LAFGIDKTDK EEKVLVFDLG GGTFDVSILE
     LADGTFEVLS TAGDNKLGGD DFDNIVVDYL VDIFKKENGI DLSSDKMAMQ RLKEAAEKAK
     KDLSSTVNAS ISLPFISAGE NGPLHLETTL SRAKFEEMTK SLVERTMVPV RQALKDAGLT
     KNDIHQVLLV GGSTRIPAVV EAVKNDLGKE PNKSVNPDEV VAMGAAIQGG VISGDGKDVL
     LLDVTPLSLG IETMGGVMTV LIERNTTIPT SKSQVFSTAA DNQPAVDINV LQGERPMAKD
     NKSLGLFKLD GIAPAKRGIP QIEVTFDIDV NGIVNVSAMD KGTNKKQSIT ISNSSGLSDE
     EIERMVREAE ENASEDLRLK EEAELKNRAE QFIHQIDESL ASEDSPVDDA QKEEVTKLRD
     ELQAAMDNND FETLKEKLDQ LEQAAQAMSQ AMYEQQAGQA EVDASSSDET VVDAEFEEKN