ID   DNAK_STRPZ              Reviewed;         608 AA.
AC   B5XHZ0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=Spy49_1374c;
OS   Streptococcus pyogenes serotype M49 (strain NZ131).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=471876;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NZ131;
RX   PubMed=18820018; DOI=10.1128/jb.00672-08;
RA   McShan W.M., Ferretti J.J., Karasawa T., Suvorov A.N., Lin S., Qin B.,
RA   Jia H., Kenton S., Najar F., Wu H., Scott J., Roe B.A., Savic D.J.;
RT   "Genome sequence of a nephritogenic and highly transformable M49 strain of
RT   Streptococcus pyogenes.";
RL   J. Bacteriol. 190:7773-7785(2008).
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; CP000829; ACI61652.1; -; Genomic_DNA.
DR   RefSeq; WP_009881037.1; NC_011375.1.
DR   AlphaFoldDB; B5XHZ0; -.
DR   SMR; B5XHZ0; -.
DR   EnsemblBacteria; ACI61652; ACI61652; Spy49_1374c.
DR   KEGG; soz:Spy49_1374c; -.
DR   HOGENOM; CLU_005965_2_4_9; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000001039; 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   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..608
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000119765"
FT   REGION          578..608
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        585..599
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         173
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   608 AA;  64978 MW;  62B2DADE7A802AF0 CRC64;
     MSKIIGIDLG TTNSAVAVLE GTESKIIANP EGNRTTPSVV SFKNGEIIVG DAAKRQAVTN
     PETVISIKSK MGTSEKVSAN GKEYTPQEIS AMILQYLKGY AEDYLGEKVE KAVITVPAYF
     NDAQRQATKD AGKIAGLEVE RIVNEPTAAA LAYGMDKTDK DEKILVFDLG GGTFDVSILE
     LGDGVFDVLA TAGDNKLGGD DFDQKIIDFL VEEFKKENGI DLSQDKMALQ RLKDAAEKAK
     KDLSGVTQTQ ISLPFITAGS AGPLHLEMSL SRAKFDDLTR DLVERTKTPV RQALSDAGLS
     LSEIDEVILV GGSTRIPAVV EAVKAETGKE PNKSVNPDEV VAMGAAIQGG VITGDVKDVV
     LLDVTPLSLG IETMGGVFTK LIDRNTTIPT SKSQVFSTAA DNQPAVDIHV LQGERPMAAD
     NKTLGRFQLT DIPAAPRGIP QIEVTFDIDK NGIVSVKAKD LGTQKEQHIV IKSNDGLSEE
     EIDRMMKDAE ANAEADAKRK EEVDLKNEVD QAIFATEKTI KETEGKGFDT ERDAAQSALD
     ELKAAQESGN LDDMKAKLEA LNEKAQALAV KMYEQAAAAQ QAAQGAEGAQ ANDSANNDDV
     VDGEFTEK