ID   DNAK_STRMU              Reviewed;         612 AA.
AC   O06942;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2002, sequence version 2.
DT   03-AUG-2022, entry version 134.
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=SMU_82;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-589.
RC   STRAIN=GS-5;
RX   PubMed=9282745; DOI=10.1046/j.1365-2958.1997.4671835.x;
RA   Jayaraman G.C., Penders J.E., Burne R.A.;
RT   "Transcriptional analysis of the Streptococcus mutans hrcA, grpE and dnaK
RT   genes and regulation of expression in response to heat shock and
RT   environmental acidification.";
RL   Mol. Microbiol. 25:329-341(1997).
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC   -!- INDUCTION: By heat shock.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; AE014133; AAN57867.1; -; Genomic_DNA.
DR   EMBL; U78296; AAC45612.1; -; Genomic_DNA.
DR   RefSeq; NP_720561.1; NC_004350.2.
DR   RefSeq; WP_002263417.1; NC_004350.2.
DR   AlphaFoldDB; O06942; -.
DR   SMR; O06942; -.
DR   STRING; 210007.SMU_82; -.
DR   PRIDE; O06942; -.
DR   EnsemblBacteria; AAN57867; AAN57867; SMU_82.
DR   GeneID; 66818410; -.
DR   KEGG; smu:SMU_82; -.
DR   PATRIC; fig|210007.7.peg.71; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_3_9; -.
DR   OMA; ISIKRHM; -.
DR   PhylomeDB; O06942; -.
DR   Proteomes; UP000002512; 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   2: Evidence at transcript level;
KW   ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Stress response.
FT   CHAIN           1..612
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078552"
FT   REGION          576..612
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        579..595
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        596..612
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         173
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        81
FT                   /note="G -> A (in Ref. 2; AAC45612)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        383..405
FT                   /note="DRNTTIPTSKSQVFSTAADNQPA -> IAIQQSQLLNHKSSQQTLQITNQS
FT                   (in Ref. 2; AAC45612)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        577
FT                   /note="A -> R (in Ref. 2; AAC45612)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   612 AA;  65286 MW;  2997CB83C3D57804 CRC64;
     MSKIIGIDLG TTNSAVAVLE GTESKIIANP EGNRTTPSVV SFKNGEIIVG DAAKRQAVTN
     PETILSIKSK MGTSEKVSAN GKEYTPQEIS AMILQYLKGY AEDYLGEKVE KAVITVPAYF
     NDAQRQATKD AGKIAGLEVE RIVNEPTAAA LAYGLDKTDK DEKILVFDLG GGTFDVSILE
     LGDGVFDVLA TAGDNKLGGD NFDQKVIDWL VEEFKKENGI DLSTDKMALQ RLKDAAEKAK
     KDLSGVTSTQ ISLPFITAGE AGPLHLETSL SRAKFDDLTR DLVERTKTPV RQALSDAGLS
     LSEIDEVILV GGSTRIPAVV DAVKAETGKE PNKSVNPDEV VAMGAAIQGG VITGDVKDVV
     LLDVTPLSLG IETMGGVFTK LIDRNTTIPT SKSQVFSTAA DNQPAVDIHV LQGERPMAAD
     NKTLGRFQLT DIPAAPRGVP QIEVTFDIDK NGIVSVKAKD LGTQKEQTIV IQSNSGLTDE
     EIDKMMKDAE ANAEADAKRK EEVDLKNEVD QAIFTTEKTI KETEGKGFDT ERDAAQAALD
     DLKKAQESGN LDDMKAKLEA LNEKAQALAM KLYEQAAAAQ QAQAGQEGAQ SSDSDSSDKG
     GDDVVDGEFT EK