ID   DNAK_STRPS              Reviewed;         607 AA.
AC   B2IMB5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=SPCG_0490;
OS   Streptococcus pneumoniae (strain CGSP14).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=516950;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGSP14;
RX   PubMed=19361343; DOI=10.1186/1471-2164-10-158;
RA   Ding F., Tang P., Hsu M.-H., Cui P., Hu S., Yu J., Chiu C.-H.;
RT   "Genome evolution driven by host adaptations results in a more virulent and
RT   antimicrobial-resistant Streptococcus pneumoniae serotype 14.";
RL   BMC Genomics 10:158-158(2009).
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; CP001033; ACB89742.1; -; Genomic_DNA.
DR   RefSeq; WP_000034668.1; NC_010582.1.
DR   AlphaFoldDB; B2IMB5; -.
DR   SMR; B2IMB5; -.
DR   EnsemblBacteria; ACB89742; ACB89742; SPCG_0490.
DR   KEGG; spw:SPCG_0490; -.
DR   HOGENOM; CLU_005965_2_4_9; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000001682; 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..607
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000119764"
FT   REGION          580..607
FT                   /note="Disordered"
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   607 AA;  64811 MW;  11D626E1397D17DA CRC64;
     MSKIIGIDLG TTNSAVAVLE GTESKIIANP EGNRTTPSVV SFKNGEIIVG DAAKRQAVTN
     PDTVISIKSK MGTSEKVSAN GKEYTPQEIS AMILQYLKGY AEDYLGEKVT KAVITVPAYF
     NDAQRQATKD AGKIAGLEVE RIVNEPTAAA LAYGLDKTDK EEKILVFDLG GGTFDVSILE
     LGDGVFDVLS TAGDNKLGGD DFDQKIIDHL VAEFKKENGI DLSTDKMAMQ RLKDAAEKAK
     KDLSGVTSTQ ISLPFITAGE AGPLHLEMTL TRAKFDDLTR DLVERTKVPV RQALSDAGLS
     LSEIDEVILV GGSTRIPAVV EAVKAETGKE PNKSVNPDEV VAMGAAIQGG VITGDVKDVV
     LLDVTPLSLG IETMGGVFTK LIDRNTTIPT SKSQVFSTAA DNQPAVDIHV LQGERPMAAD
     NKTLGRFQLT DIPAAPRGIP QIEVTFDIDK NGIVSVKAKD LGTQKEQTIV IQSNSGLTDE
     EIDRMMKDAE ANAEADKKRK EEVDLRNEVD QAIFATEKTI KETEGKGFDA ERDAAQAALD
     DLKKAQENNN LDDMKAKLEA LNEKAQGLAV KLYEQAAAAQ QAQEGAEGAQ ATGNAGDDVV
     DGEFTEK