ID   DNAK_RHOMR              Reviewed;         640 AA.
AC   Q9XCB1;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Chaperone protein DnaK;
DE   AltName: Full=HSP70;
DE   AltName: Full=Heat shock 70 kDa protein;
DE   AltName: Full=Heat shock protein 70;
GN   Name=dnaK;
OS   Rhodothermus marinus (Rhodothermus obamensis).
OC   Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis;
OC   Rhodothermaceae; Rhodothermus.
OX   NCBI_TaxID=29549;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ITI 376;
RA   Thorolfsdottir E.T.T., Backman V.M., Blondal T., Thorbjarnardottir S.H.,
RA   Palsdottir A., Hauksdottir H., Kristjansdottir S., Eggertsson G.;
RT   "Heat shock in Rhodothermus marinus: cloning and sequence analysis of the
RT   groESL, dnaK and dnaJ genes.";
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC   -!- INDUCTION: By stress conditions e.g. heat shock (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; AF145251; AAD37974.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9XCB1; -.
DR   SMR; Q9XCB1; -.
DR   PRIDE; Q9XCB1; -.
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; 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   Stress response.
FT   CHAIN           1..640
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078527"
FT   REGION          600..640
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        600..618
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        626..640
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         201
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   640 AA;  70201 MW;  9F1A2A5E8F644FE1 CRC64;
     MGKIIGIDLG TTNSVVAVME GGEPKVIINP EGSRVTPSVV AFTADGEPLV GAPAKRQAIT
     NPKNTIFSIK RFMGRFYDEV TEEISMVPYK VVRGENNTVR VEVEVGGEKR LYTPQEISAM
     ILQKLKQTAE EYLGVPVTEA VITVPAYFND AQRKATKEAG EIAGLKVRRI LNEPTAAALA
     YGLDKKDKEL KIAVYDLGGG TYDISILELG DGVFEVKATN GDTHLGGDNF DQRLIDYIAD
     EFQKQEGIDL RKDPMALQRL KEAAEKAKIE LSSAMKTTVN LPFITATAEG PKHLVMEITR
     AKFEQLIEDL VARTIPPMEQ ALKDAKLRKE DIDEVILVGG STRIPLVQRT VEEFFGKKAN
     KSVNPDEVVA IGAAIQAGVL SGEVQDVLLL DVTPLNLGIE TLGGVMTVLI PANTTIPTRK
     SEIFTTASDN QTSVEIHVLQ GNREMAADNR SLGRFILDGI PPAPRGVPQI EVTFDIDANG
     ILHVSARDKA TGKEQSIRIE ASSGLTPEEI ERMREEARRH AAEDRKRREQ IEKLNQADSL
     IYMTEKNLRE YGDKLPADKR AKIESALERL KEVHKARNFD ELDSAIAQLN QAWNEASQDL
     YRAQQAAGAQ TSDGASAQAD SGGVREADYE VIDEDDKDKQ