ID   DNAK_SULNB              Reviewed;         627 AA.
AC   A6QBG0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=SUN_1872;
OS   Sulfurovum sp. (strain NBC37-1).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Sulfurovaceae; Sulfurovum; unclassified Sulfurovum.
OX   NCBI_TaxID=387093;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBC37-1;
RX   PubMed=17615243; DOI=10.1073/pnas.0700687104;
RA   Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K.,
RA   Horikoshi K.;
RT   "Deep-sea vent epsilon-proteobacterial genomes provide insights into
RT   emergence of pathogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(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; AP009179; BAF72819.1; -; Genomic_DNA.
DR   RefSeq; WP_012083632.1; NC_009663.1.
DR   AlphaFoldDB; A6QBG0; -.
DR   SMR; A6QBG0; -.
DR   STRING; 387093.SUN_1872; -.
DR   PRIDE; A6QBG0; -.
DR   EnsemblBacteria; BAF72819; BAF72819; SUN_1872.
DR   KEGG; sun:SUN_1872; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_7; -.
DR   OMA; DKMVLQR; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000006378; 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; PS01036; HSP70_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Stress response.
FT   CHAIN           1..627
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059689"
FT   REGION          598..627
FT                   /note="Disordered"
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   627 AA;  66826 MW;  8A05D404ED11052F CRC64;
     MGKVLGIDLG TTNSAMAVYT NGEAAIIANK EGKNTTPSIV AFTDKGEVLV GESAKRQAVT
     NPEKTIYSIK RIMGLMCEEE KANEAKERLP YHIIDRNGAC AIEVAGKTYT PQEISAKVLM
     KMKEDAEAYL GETVTDAVIT VPAYFNDAQR KATKEAGTIA GLNVLRIINE PTSAALAYGL
     DKKEAEQIVV YDLGGGTFDV TALETGDGVV EVLATGGDAF LGGDDFDNRI IDYVADEFKS
     ESGIDIKADV MALQRVKDAA EAAKKELSSA TETEINLPFI TADASGPKHL VTKITRAKFE
     SLIGDLVAKT IKTIEAVLKD AGLSKNDVKE VVMVGGSTRV PLVQEEVKKF FNKELNKSVN
     PDEVVALGAA IQGGVLAGDV KDVLLLDVTP LSLGIETLGG VMTKVIEKGT TIPAKKSQIF
     STAEDNQPAV SIHVLQGERE FAKDNKSLGM FELRDIPAAP RGVPQIEVTF DIDANGILTV
     SAVDKGTGKS QEIKITGSSG LSDEEIEKMV QDAEAHKAED EKRKAVVEAK NQADALIHQT
     KKSLDDLGEN FDANEKAGIE AAIADLETVL KDDNATKEQI DEKVKALTEK SHKLAEAAYA
     KEQGGQQGAA DAGKKADDDD VIDAEVE