ID   DNAK_SULDN              Reviewed;         628 AA.
AC   Q30Q10;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=Suden_1644;
OS   Sulfurimonas denitrificans (strain ATCC 33889 / DSM 1251) (Thiomicrospira
OS   denitrificans (strain ATCC 33889 / DSM 1251)).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Thiovulaceae; Sulfurimonas.
OX   NCBI_TaxID=326298;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33889 / DSM 1251;
RX   PubMed=18065616; DOI=10.1128/aem.01844-07;
RA   Sievert S.M., Scott K.M., Klotz M.G., Chain P.S.G., Hauser L.J., Hemp J.,
RA   Huegler M., Land M., Lapidus A., Larimer F.W., Lucas S., Malfatti S.A.,
RA   Meyer F., Paulsen I.T., Ren Q., Simon J., Bailey K., Diaz E.,
RA   Fitzpatrick K.A., Glover B., Gwatney N., Korajkic A., Long A.,
RA   Mobberley J.M., Pantry S.N., Pazder G., Peterson S., Quintanilla J.D.,
RA   Sprinkle R., Stephens J., Thomas P., Vaughn R., Weber M.J., Wooten L.L.;
RT   "Genome of the epsilonproteobacterial chemolithoautotroph Sulfurimonas
RT   denitrificans.";
RL   Appl. Environ. Microbiol. 74:1145-1156(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; CP000153; ABB44921.1; -; Genomic_DNA.
DR   RefSeq; WP_011373262.1; NC_007575.1.
DR   AlphaFoldDB; Q30Q10; -.
DR   SMR; Q30Q10; -.
DR   STRING; 326298.Suden_1644; -.
DR   PRIDE; Q30Q10; -.
DR   EnsemblBacteria; ABB44921; ABB44921; Suden_1644.
DR   KEGG; tdn:Suden_1644; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_7; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000002714; 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; 1.
DR   Pfam; PF00012; HSP70; 1.
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.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Stress response.
FT   CHAIN           1..628
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000072042"
FT   REGION          597..628
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        613..628
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         197
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   628 AA;  67046 MW;  8AC84862B3917019 CRC64;
     MSKVIGIDLG TTNSCVAVYE GGEAKIIPNK EGKNTTPSIV AFTDKGEVLV GDPAKRQAIT
     NPNKTISSIK RIMGLMMSEE NAKAAHDKVT YNIVDKDGMA AVDVAGKIYT PQEISAKILS
     KLKEDAEAYI GSSVTDAVIT VPAYFNDAQR KATKDAGTIA GLNVLRIINE PTASALAYGL
     ESKSDENVLV YDLGGGTFDV TVLEISDGTF EVLSTDGNAF LGGDDFDNKI VDYLNAEFKS
     SHGIDLKNDK MALQRLKDAA ENAKKELSSS TETEINLPFI TMTEAGPQHL VLKLTRAKFE
     SMIEKLVEET IAHIKTAMKE SGLDNDAIKE IIMVGGSTRV PLAQEMVSKF FGGKKLNKGV
     NPDEVVAAGA AIQGGVLRGD VKDVLLLDVT PLSLGIETLG GVATKIIEKG TTIPVKKSQI
     FSTAEDNQPA VSISVVQGER EFARDNKSLG LFELGNIAAA PRGVPQIEVT FDIDANGILT
     VSSTDKGTGK SQSITISGSS GLSEEEINKM VKDAELHKAE DSKRKELVEL KNQADALIAQ
     TEKSIGEMGD KIEADEKAKI EAAITELKDV LKDTNATKEK IEPKVKTLTE ASHKMAEQMY
     KGEQGAQGGA ADTSKKKSDD DVIDAEIE