ID   DNAK_RUBXD              Reviewed;         636 AA.
AC   Q1AXX6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=Rxyl_0784;
OS   Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129 / PRD-1).
OC   Bacteria; Actinobacteria; Rubrobacteria; Rubrobacterales; Rubrobacteraceae;
OC   Rubrobacter.
OX   NCBI_TaxID=266117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9941 / NBRC 16129 / PRD-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., da Costa M.S.,
RA   Rainey F.A., Empadinhas N., Jolivet E., Battista J.R., Richardson P.;
RT   "Complete sequence of Rubrobacter xylanophilus DSM 9941.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000386; ABG03752.1; -; Genomic_DNA.
DR   RefSeq; WP_011563770.1; NC_008148.1.
DR   AlphaFoldDB; Q1AXX6; -.
DR   SMR; Q1AXX6; -.
DR   STRING; 266117.Rxyl_0784; -.
DR   PRIDE; Q1AXX6; -.
DR   EnsemblBacteria; ABG03752; ABG03752; Rxyl_0784.
DR   KEGG; rxy:Rxyl_0784; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_11; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   PhylomeDB; Q1AXX6; -.
DR   Proteomes; UP000006637; 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..636
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059653"
FT   REGION          596..636
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        596..613
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        615..636
FT                   /note="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   636 AA;  69174 MW;  E126F1B158139844 CRC64;
     MGKSIGIDLG TTNSCVAVLE GGDPVVIPNA EGERTTPSVV AFDRKSGERL VGQLARRQAV
     TNPERTVYSI KRFMGRRYND VKQEAERVGY QVVPGPHGDV RVRLGDKDYS PPEISAMILQ
     KLKRDAEDYL GEEVTDAVIT VPAYFEDAQR QATKDAGRIA GLNVKRIINE PTAAALAYGL
     DKENDQTILV FDLGGGTFDV SILELGDGVF EVKATSGNNH LGGDDFDAKV VEWIVEEFKK
     AEGIDLSRDK MAMQRLVEAA EKAKKELSST TSTNINLPFI TADANGPKHL DLTLTRAQFN
     KLTADLVEAT AGPVRQAMQD AGLKPGDVDQ VILVGGSTRI PAVQEKVKEL TGKEPHKGIN
     PDEVVAIGAA IQAGVLAGEV KDVLLLDVTP LSLGIETKGG VFTKLIERNT TIPTRKSEIF
     TTAEDNQQSV EIKVYQGERE IAAHNKLIGN FQLVGIPPAP RGVPQIEVTF DIDANGILNV
     GAKDLGTGKE QKITITASSG LSDQEIEQMV RDAEAHAEED RRKREEAEIR NNADNLVYSV
     ERSLKEVDGK VDSSTREEIE KAIKEAKEAL AGDDIEEIKR KQEALMSASH KLSQVLYQQA
     QEQQQSGSSG GSSDEDVVED AEIVDEEDEE KRDDNR