ID   DNAK_STRGC              Reviewed;         607 AA.
AC   A8AVA8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=SGO_0402;
OS   Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 /
OS   DL1 / V288).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=467705;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288;
RX   PubMed=17720781; DOI=10.1128/jb.01023-07;
RA   Vickerman M.M., Iobst S., Jesionowski A.M., Gill S.R.;
RT   "Genome-wide transcriptional changes in Streptococcus gordonii in response
RT   to competence signaling peptide.";
RL   J. Bacteriol. 189:7799-7807(2007).
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; CP000725; ABV10760.1; -; Genomic_DNA.
DR   RefSeq; WP_011999914.1; NC_009785.1.
DR   AlphaFoldDB; A8AVA8; -.
DR   SMR; A8AVA8; -.
DR   STRING; 467705.SGO_0402; -.
DR   EnsemblBacteria; ABV10760; ABV10760; SGO_0402.
DR   KEGG; sgo:SGO_0402; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_9; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000001131; 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   Reference proteome; Stress response.
FT   CHAIN           1..607
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000079251"
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;  64724 MW;  4534557E45C70400 CRC64;
     MSKIIGIDLG TTNSAVAVLE GTESKIIANP EGNRTTPSVV SFKNGEIIVG DAAKRQAVTN
     PDTVISIKSK MGTSEKVSAN GKEYTPQEIS AMILQYLKGY AEEYLGEKVT KAVITVPAYF
     NDAQRQATKD AGKIAGLEVE RIVNEPTAAA LAYGLDKTDK EEKILVFDLG GGTFDVSILE
     LGDGVFDVLA TAGDNKLGGD DFDQKIIDHM VAEFKKENGI DLSTDKMALQ RLKDAAEKAK
     KDLSGVTSTQ ISLPFITAGA AGPLHLEMTL TRAKFDDLTR DLVERTKTPV 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
     DLKKAQEDNK LDEMKAKLEA LNEKAQGLAV KLYEQAAAAQ QAQAGAEGAQ ATGNAGDDVV
     DGEFTEK