ID   DNAK_IDILO              Reviewed;         642 AA.
AC   Q5QXL1;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-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=IL0986;
OS   Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Idiomarina.
OX   NCBI_TaxID=283942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR;
RX   PubMed=15596722; DOI=10.1073/pnas.0407638102;
RA   Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y.,
RA   Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S.,
RA   Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S.,
RA   Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.;
RT   "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina
RT   loihiensis reveals amino acid fermentation as a source of carbon and
RT   energy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004).
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; AE017340; AAV81826.1; -; Genomic_DNA.
DR   RefSeq; WP_011234237.1; NC_006512.1.
DR   AlphaFoldDB; Q5QXL1; -.
DR   SMR; Q5QXL1; -.
DR   STRING; 283942.IL0986; -.
DR   PRIDE; Q5QXL1; -.
DR   EnsemblBacteria; AAV81826; AAV81826; IL0986.
DR   KEGG; ilo:IL0986; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000001171; 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.
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..642
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000225970"
FT   REGION          570..642
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        570..587
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        598..616
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         199
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   642 AA;  69403 MW;  535A8B087E660C43 CRC64;
     MGKTIGIDLG TTNSCVAVLD GGKARVIENG EGDRTTPSVV AFTDDGEILV GSPAKRQAVT
     NPNKTLFAIK RLIGRRFQDE EVQRDIGIMP YKIVKADNGD AWVEIDGDKK APPQISAEVL
     KKMKKTAEEF LGEKVTDAVI TVPAYFNDAQ RQATKDAGKI AGLNVKRIIN EPTAAALAYG
     MDKKSGDNVI AVYDLGGGTF DISIIEIDEV EGEHTFEVLA TNGDTHLGGE DFDNRLINYL
     VEQFQKDQGM DLRKDPLAMQ RLKEAAEKAK IELSSAQQTE VNLPYITADN AGPKHMAIKV
     TRAKLESLVE DLIKKSLEPL KQALADADLS VSDIQDIIMV GGQTRMPKVQ AAVTDFFGKE
     PRRDVNPDEA VAVGAAVQAG VLQGDVKDVL LLDVCPLSLG IETMGGVMTK LIEKNTTIPT
     KESQTFSTAE DNQSAVTIHV IQGERKRAGD NKSLGQFNLE GIRAAARGVP QIEVTFDIDA
     DGILHVSAKD KDTGKEQKIT IKASSGLDES EVDKMVKDAE AHAEEDKKFE EMVQARNQAD
     GLVHATRNQL KEVGDALSQE DKDAIEKACE ELEQASKDGD KEAIDAKSQA LMEASQKLME
     AAQQQQAQQG AEGAAGGEQQ SSKADDDVVD AEFEEVKDDD KK