ID   DNAK_STRPN              Reviewed;         607 AA.
AC   P95829; O66035;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2001, sequence version 2.
DT   03-AUG-2022, entry version 132.
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; OrderedLocusNames=SP_0517;
OS   Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=170187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Rioux C.R., Martin D., Hamel J., Brodeur B.R.;
RT   "Heat shock protein HSP70 and amino terminus of DnaJ of Streptococcus
RT   pneumoniae.";
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Rx / CP1200;
RX   PubMed=9570114; DOI=10.1111/j.1574-6968.1998.tb12951.x;
RA   Kim S.-W., Choi I.-H., Kim S.-N., Kim Y.-H., Pyo S.-N., Rhee D.-K.;
RT   "Molecular cloning, expression, and characterization of dnaK in
RT   Streptococcus pneumoniae.";
RL   FEMS Microbiol. Lett. 161:217-224(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-334 / TIGR4;
RX   PubMed=11463916; DOI=10.1126/science.1061217;
RA   Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA   Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA   Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA   Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA   Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA   McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA   Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA   Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT   "Complete genome sequence of a virulent isolate of Streptococcus
RT   pneumoniae.";
RL   Science 293:498-506(2001).
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; U72720; AAB39221.1; -; Genomic_DNA.
DR   EMBL; U84387; AAC15892.1; -; Genomic_DNA.
DR   EMBL; AE005672; AAK74675.1; -; Genomic_DNA.
DR   PIR; B95060; B95060.
DR   RefSeq; WP_000034665.1; NZ_AKVY01000001.1.
DR   AlphaFoldDB; P95829; -.
DR   SMR; P95829; -.
DR   STRING; 170187.SP_0517; -.
DR   EnsemblBacteria; AAK74675; AAK74675; SP_0517.
DR   KEGG; spn:SP_0517; -.
DR   eggNOG; COG0443; Bacteria.
DR   OMA; ISIKRHM; -.
DR   PhylomeDB; P95829; -.
DR   BioCyc; SPNE170187:G1FZB-532-MON; -.
DR   Proteomes; UP000000585; 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_0000078553"
FT   REGION          581..607
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         173
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        493
FT                   /note="A -> P (in Ref. 2; AAC15892)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        495
FT                   /note="A -> S (in Ref. 1; AAB39221)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        530
FT                   /note="A -> P (in Ref. 2; AAC15892)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        556
FT                   /note="T -> A (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        601..602
FT                   /note="DG -> E (in Ref. 2; AAC15892)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   607 AA;  64842 MW;  11D626F1837D0760 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
     DLKKAQEDNN LDDMKTKLEA LNEKAQGLAV KLYEQAAAAQ QAQEGAEGAQ ATGNAGDDVV
     DGEFTEK